SYC_YEAST
ID SYC_YEAST Reviewed; 767 AA.
AC P53852; D6W0U6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16 {ECO:0000269|PubMed:9523015};
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN OrderedLocusNames=YNL247W; ORFNames=N0885;
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 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 137-164; 247-269 AND 407-416, FUNCTION, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9523015; DOI=10.1016/s0300-9084(97)86931-3;
RA Motorin Y., Le Caer J.-P., Waller J.-P.;
RT "Cysteinyl-tRNA synthetase from Saccharomyces cerevisiae. Purification,
RT characterization and assignment to the genomic sequence YNL247w.";
RL Biochimie 79:731-740(1997).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC Evidence={ECO:0000269|PubMed:9523015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC Evidence={ECO:0000305|PubMed:9523015};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9523015}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 23000 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X96722; CAA65497.1; -; Genomic_DNA.
DR EMBL; Z71523; CAA96154.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10312.1; -; Genomic_DNA.
DR PIR; S63220; S63220.
DR RefSeq; NP_014152.1; NM_001183085.1.
DR AlphaFoldDB; P53852; -.
DR SMR; P53852; -.
DR BioGRID; 35592; 63.
DR IntAct; P53852; 4.
DR MINT; P53852; -.
DR STRING; 4932.YNL247W; -.
DR iPTMnet; P53852; -.
DR MaxQB; P53852; -.
DR PaxDb; P53852; -.
DR PRIDE; P53852; -.
DR EnsemblFungi; YNL247W_mRNA; YNL247W; YNL247W.
DR GeneID; 855474; -.
DR KEGG; sce:YNL247W; -.
DR SGD; S000005191; YNL247W.
DR VEuPathDB; FungiDB:YNL247W; -.
DR eggNOG; KOG2007; Eukaryota.
DR GeneTree; ENSGT00390000006347; -.
DR HOGENOM; CLU_013528_3_1_1; -.
DR InParanoid; P53852; -.
DR OMA; FHNDMKS; -.
DR BioCyc; YEAST:G3O-33244-MON; -.
DR PRO; PR:P53852; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53852; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:SGD.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Direct protein sequencing; Ligase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..767
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159553"
FT REGION 683..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 65..75
FT /note="'HIGH' region"
FT MOTIF 427..431
FT /note="'KMSKS' region"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 767 AA; 87530 MW; 495D526781B4BE2B CRC64;
MNIFIKALRR YTIMSTPKIV QPKWKVPTPQ AKETVLKLYN SLTRSKVEFI PQSGNRGVTW
YSCGPTVYDA SHMGHARNYV SIDINRRIIQ DYFGYDVQFV QNVTDIDDKI ILRARQNYLF
DNFVKENDTK FNATVVDKVK TALFQYINKN FTIQGSEIKT IEEFETWLSN ADTETLKLEN
PKFPMHVTAV QNAIESITKG DSMDAEVAFE KVKDVTVPLL DKELGSTISN PEIFRQLPAY
WEQKFNDDML SLNVLPPTVT TRVSEYVPEI IDFVQKIIDN GYAYATSDGS VYFDTLKFDK
SPNHDYAKCQ PWNKGQLDLI NDGEGSLSNF ADNGKKSNND FALWKASKAG EPEWESPWGK
GRPGWHIECS VMASDILGSN IDIHSGGIDL AFPHHDNELA QSEARFDNQQ WINYFLHTGH
LHIEGQKMSK SLKNFITIQE ALKKFSPRQL RLAFASVQWN NQLDFKESLI HEVKSFENSM
NNFFKTIRAL KNDAASAGHI SKKFSPLEKE LLADFVESES KVHSAFCDNL STPVALKTLS
ELVTKSNTYI TTAGAALKIE PLIAICSYIT KILRIIGFPS RPDNLGWAAQ AGSNDGSLGS
LEDTVMPYVK CLSTFRDDVR SLAIKKAEPK EFLQLTDKIR NEDLLNLNVA LDDRNGQSAL
IKFLTNDEKL EIVKLNEEKH ANELAKKQKK LEQQKLREQK ENERKQKAQI KPQDMFKDVT
LYSAWDEQGL PTKDKDGNDI TKSMTKKLKK QWEQQKKLHE EYFGEDK
