SYWC_YEAST
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 03-AUG-2022, entry version 167.
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; 241.
DR DIP; DIP-6750N; -.
DR IntAct; Q12109; 2.
DR MINT; Q12109; -.
DR STRING; 4932.YOL097C; -.
DR iPTMnet; Q12109; -.
DR MaxQB; Q12109; -.
DR PaxDb; Q12109; -.
DR PRIDE; Q12109; -.
DR EnsemblFungi; YOL097C_mRNA; YOL097C; YOL097C.
DR GeneID; 854056; -.
DR KEGG; sce:YOL097C; -.
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 BioCyc; YEAST:G3O-33496-MON; -.
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; -; 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 Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 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
