ID   SYWC_YEAST              Reviewed;         432 AA.
AC   Q12109; D6W1X1; E9P8Z9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Tryptophan--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.2 {ECO:0000269|PubMed:9046085};
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
GN   Name=WRS1; OrderedLocusNames=YOL097C; ORFNames=HRE432;
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].
RX   PubMed=7502582; DOI=10.1002/yea.320111108;
RA   Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT   the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT   tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL   Yeast 11:1069-1075(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9046085;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<37::aid-yea55>3.0.co;2-l;
RA   John T.R., Ghosh M., Johnson J.D.;
RT   "Identification and expression of the Saccharomyces cerevisiae cytoplasmic
RT   tryptophanyl-tRNA synthetase gene.";
RL   Yeast 13:37-41(1997).
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   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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC         Evidence={ECO:0000269|PubMed:9046085};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24081;
CC         Evidence={ECO:0000305|PubMed:9046085};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 12100 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; Z48149; CAA88164.1; -; Genomic_DNA.
DR   EMBL; Z74839; CAA99110.1; -; Genomic_DNA.
DR   EMBL; AY692948; AAT92967.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10687.1; -; Genomic_DNA.
DR   PIR; S51901; S51901.
DR   RefSeq; NP_014544.1; NM_001183351.1.
DR   PDB; 2IP1; X-ray; 1.80 A; A=1-432.
DR   PDB; 3KT0; X-ray; 2.10 A; A=1-432.
DR   PDB; 3KT3; X-ray; 2.60 A; A/B/C/D=1-432.
DR   PDB; 3KT6; X-ray; 2.80 A; A/B/C/D=1-432.
DR   PDB; 3KT8; X-ray; 3.00 A; A/B/C/D=1-432.
DR   PDBsum; 2IP1; -.
DR   PDBsum; 3KT0; -.
DR   PDBsum; 3KT3; -.
DR   PDBsum; 3KT6; -.
DR   PDBsum; 3KT8; -.
DR   AlphaFoldDB; Q12109; -.
DR   SMR; Q12109; -.
DR   BioGRID; 34305; 245.
DR   DIP; DIP-6750N; -.
DR   IntAct; Q12109; 2.
DR   MINT; Q12109; -.
DR   STRING; 4932.YOL097C; -.
DR   iPTMnet; Q12109; -.
DR   MaxQB; Q12109; -.
DR   PaxDb; 4932-YOL097C; -.
DR   PeptideAtlas; Q12109; -.
DR   EnsemblFungi; YOL097C_mRNA; YOL097C; YOL097C.
DR   GeneID; 854056; -.
DR   KEGG; sce:YOL097C; -.
DR   AGR; SGD:S000005457; -.
DR   SGD; S000005457; WRS1.
DR   VEuPathDB; FungiDB:YOL097C; -.
DR   eggNOG; KOG2145; Eukaryota.
DR   GeneTree; ENSGT00940000153724; -.
DR   HOGENOM; CLU_032621_0_1_1; -.
DR   InParanoid; Q12109; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 540846at2759; -.
DR   BioCyc; YEAST:G3O-33496-MONOMER; -.
DR   BioGRID-ORCS; 854056; 9 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q12109; -.
DR   PRO; PR:Q12109; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12109; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   NCBIfam; TIGR00233; trpS; 1.
DR   PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..432
FT                   /note="Tryptophan--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000136744"
FT   MOTIF           111..120
FT                   /note="'HIGH' region"
FT   MOTIF           295..299
FT                   /note="'KMSKS' region"
FT   CONFLICT        87
FT                   /note="E -> G (in Ref. 4; AAT92967)"
FT                   /evidence="ECO:0000305"
FT   HELIX           47..54
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:3KT3"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           144..150
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           185..188
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           191..201
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           206..211
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           221..225
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           227..232
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   TURN            240..243
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          251..256
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           260..273
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          279..283
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:3KT6"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           311..321
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           330..336
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           344..352
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           356..367
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           373..396
FT                   /evidence="ECO:0007829|PDB:2IP1"
FT   HELIX           400..407
FT                   /evidence="ECO:0007829|PDB:2IP1"
SQ   SEQUENCE   432 AA;  49350 MW;  C408F169737E9736 CRC64;
     MSNDETVEKV TQQVSELKST DVKEQVVTPW DVEGGVDEQG RAQNIDYDKL IKQFGTKPVN
     EETLKRFKQV TGREPHHFLR KGLFFSERDF TKILDLYEQG KPFFLYTGRG PSSDSMHLGH
     MIPFVFTKWL QEVFDVPLVI ELTDDEKFLF KHKLTINDVK NFARENAKDI IAVGFDPKNT
     FIFSDLQYMG GAFYETVVRV SRQITGSTAK AVFGFNDSDC IGKFHFASIQ IATAFPSSFP
     NVLGLPDKTP CLIPCAIDQD PYFRVCRDVA DKLKYSKPAL LHSRFFPALQ GSTTKMSASD
     DTTAIFMTDT PKQIQKKINK YAFSGGQVSA DLHRELGGNP DVDVAYQYLS FFKDDDVFLK
     ECYDKYKSGE LLSGEMKKLC IETLQEFVKA FQERRAQVDE ETLDKFMVPH KLVWGEKERL
     VAPKPKTKQE KK
//