SYIC_YEAST
ID SYIC_YEAST Reviewed; 1072 AA.
AC P09436; D6VPS6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Isoleucine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
GN Name=ILS1; OrderedLocusNames=YBL076C; ORFNames=YBL0734;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=2663194; DOI=10.1007/bf00435455;
RA Martindale D.W., Gu Z.M., Csank C.;
RT "Isolation and complete sequence of the yeast isoleucyl-tRNA synthetase
RT gene (ILS1).";
RL Curr. Genet. 15:99-106(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=3311074; DOI=10.1515/bchm3.1987.368.2.971;
RA Englisch U., Englisch E., Markmeyer P., Schischkoff J., Sternbach H.,
RA Kratzin H., Cramer F.;
RT "Structure of the yeast isoleucyl-tRNA synthetase gene (ILS1). DNA-
RT sequence, amino-acid sequence of proteolytic peptides of the enzyme and
RT comparison of the structure to those of other known aminoacyl-tRNA
RT synthetases.";
RL Biol. Chem. Hoppe-Seyler 368:971-979(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829 AND SER-1059, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1059, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 23300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X07886; CAA30733.1; -; Genomic_DNA.
DR EMBL; M19992; AAA34712.1; -; Genomic_DNA.
DR EMBL; X79489; CAA56034.1; -; Genomic_DNA.
DR EMBL; Z35838; CAA84898.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07046.1; -; Genomic_DNA.
DR PIR; S14459; SYBYI4.
DR RefSeq; NP_009477.1; NM_001178316.1.
DR PDB; 7D5C; X-ray; 1.90 A; A=1-984.
DR PDBsum; 7D5C; -.
DR AlphaFoldDB; P09436; -.
DR SMR; P09436; -.
DR BioGRID; 32626; 206.
DR DIP; DIP-6388N; -.
DR IntAct; P09436; 16.
DR MINT; P09436; -.
DR STRING; 4932.YBL076C; -.
DR CarbonylDB; P09436; -.
DR iPTMnet; P09436; -.
DR MaxQB; P09436; -.
DR PaxDb; P09436; -.
DR PRIDE; P09436; -.
DR EnsemblFungi; YBL076C_mRNA; YBL076C; YBL076C.
DR GeneID; 852202; -.
DR KEGG; sce:YBL076C; -.
DR SGD; S000000172; ILS1.
DR VEuPathDB; FungiDB:YBL076C; -.
DR eggNOG; KOG0434; Eukaryota.
DR GeneTree; ENSGT00550000074921; -.
DR HOGENOM; CLU_001493_1_1_1; -.
DR InParanoid; P09436; -.
DR OMA; KMMAPFT; -.
DR BioCyc; YEAST:G3O-28968-MON; -.
DR BRENDA; 6.1.1.5; 984.
DR PRO; PR:P09436; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P09436; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IDA:SGD.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR42780; PTHR42780; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Ligase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..1072
FT /note="Isoleucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000098604"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 602..606
FT /note="'KMSKS' region"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 551
FT /note="D -> E (in Ref. 2; AAA34712)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="N -> KS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 693..695
FT /note="DRW -> AEM (in Ref. 2; AAA34712)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="F -> V (in Ref. 2; AAA34712)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="G -> V (in Ref. 2; AAA34712)"
FT /evidence="ECO:0000305"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 112..136
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 197..211
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 388..400
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 409..418
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 528..533
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 539..544
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 569..581
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 605..608
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 613..619
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 622..630
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 644..653
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 655..676
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 691..712
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 716..718
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 719..732
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 734..742
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 743..746
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 748..769
FT /evidence="ECO:0007829|PDB:7D5C"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 774..784
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 785..787
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 790..793
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 813..815
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 818..841
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 849..855
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 859..867
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 869..875
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 878..885
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 888..890
FT /evidence="ECO:0007829|PDB:7D5C"
FT HELIX 955..959
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 962..969
FT /evidence="ECO:0007829|PDB:7D5C"
FT STRAND 971..975
FT /evidence="ECO:0007829|PDB:7D5C"
SQ SEQUENCE 1072 AA; 122984 MW; 75E07F3B0A4DBBFF CRC64;
MSESNAHFSF PKEEEKVLSL WDEIDAFHTS LELTKDKPEF SFFDGPPFAT GTPHYGHILA
STIKDIVPRY ATMTGHHVER RFGWDTHGVP IEHIIDKKLG ITGKDDVFKY GLENYNNECR
SIVMTYASDW RKTIGRLGRW IDFDNDYKTM YPSFMESTWW AFKQLHEKGQ VYRGFKVMPY
STGLTTPLSN FEAQQNYKDV NDPAVTIGFN VIGQEKTQLV AWTTTPWTLP SNLSLCVNAD
FEYVKIYDET RDRYFILLES LIKTLYKKPK NEKYKIVEKI KGSDLVGLKY EPLFPYFAEQ
FHETAFRVIS DDYVTSDSGT GIVHNAPAFG EEDNAACLKN GVISEDSVLP NAIDDLGRFT
KDVPDFEGVY VKDADKLIIK YLTNTGNLLL ASQIRHSYPF CWRSDTPLLY RSVPAWFVRV
KNIVPQMLDS VMKSHWVPNT IKEKRFANWI ANARDWNVSR NRYWGTPIPL WVSDDFEEVV
CVGSIKELEE LTGVRNITDL HRDVIDKLTI PSKQGKGDLK RIEEVFDCWF ESGSMPYASQ
HYPFENTEKF DERVPANFIS EGLDQTRGWF YTLAVLGTHL FGSVPYKNVI VSGIVLAADG
RKMSKSLKNY PDPSIVLNKY GADALRLYLI NSPVLKAESL KFKEEGVKEV VSKVLLPWWN
SFKFLDGQIA LLKKMSNIDF QYDDSVKSDN VMDRWILASM QSLVQFIHEE MGQYKLYTVV
PKLLNFIDEL TNWYIRFNRR RLKGENGVED CLKALNSLFD ALFTFVRAMA PFTPFLSESI
YLRLKEYIPE AVLAKYGKDG RSVHFLSYPV VKKEYFDEAI ETAVSRMQSV IDLGRNIREK
KTISLKTPLK TLVILHSDES YLKDVEALKN YIIEELNVRD VVITSDEAKY GVEYKAVADW
PVLGKKLKKD AKKVKDALPS VTSEQVREYL ESGKLEVAGI ELVKGDLNAI RGLPESAVQA
GQETRTDQDV LIIMDTNIYS ELKSEGLARE LVNRIQKLRK KCGLEATDDV LVEYELVKDT
IDFEAIVKEH FDMLSKTCRS DIAKYDGSKT DPIGDEEQSI NDTIFKLKVF KL
