SYWM_YEAST
ID SYWM_YEAST Reviewed; 379 AA.
AC P04803; D6VSQ2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE EC=6.1.1.2 {ECO:0000305|PubMed:2999114};
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
GN Name=MSW1; Synonyms=MSW; OrderedLocusNames=YDR268W; ORFNames=D9954.7;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2999114; DOI=10.1016/s0021-9258(18)95746-7;
RA Myers A.M., Tzagoloff A.;
RT "MSW, a yeast gene coding for mitochondrial tryptophanyl-tRNA synthetase.";
RL J. Biol. Chem. 260:15371-15377(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1525855; DOI=10.1007/bf00351683;
RA Entrup R., Langgut W., Lisowsky T., Schweizer E.;
RT "An yeast nuclear mutation conferring temperature-sensitivity to the
RT mitochondrial tryptophanyl-tRNA synthetase.";
RL Curr. Genet. 21:281-283(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the
CC attachment of tryptophan to tRNA(Trp). {ECO:0000305|PubMed:2999114}.
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:0000305|PubMed:2999114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24081;
CC Evidence={ECO:0000305|PubMed:2999114};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M12081; AAA34809.1; -; Genomic_DNA.
DR EMBL; X66165; CAA46947.1; -; Genomic_DNA.
DR EMBL; U51030; AAB64452.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12112.1; -; Genomic_DNA.
DR PIR; S70128; YWBYM.
DR RefSeq; NP_010554.1; NM_001180576.1.
DR AlphaFoldDB; P04803; -.
DR SMR; P04803; -.
DR BioGRID; 32324; 22.
DR DIP; DIP-4584N; -.
DR IntAct; P04803; 6.
DR STRING; 4932.YDR268W; -.
DR MaxQB; P04803; -.
DR PaxDb; P04803; -.
DR PRIDE; P04803; -.
DR EnsemblFungi; YDR268W_mRNA; YDR268W; YDR268W.
DR GeneID; 851861; -.
DR KEGG; sce:YDR268W; -.
DR SGD; S000002676; MSW1.
DR VEuPathDB; FungiDB:YDR268W; -.
DR eggNOG; KOG2713; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_029244_1_3_1; -.
DR InParanoid; P04803; -.
DR OMA; GWGQFKP; -.
DR BioCyc; YEAST:G3O-29838-MON; -.
DR PRO; PR:P04803; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P04803; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IMP:SGD.
DR GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; IMP: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 Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..379
FT /note="Tryptophan--tRNA ligase, mitochondrial"
FT /id="PRO_0000136745"
FT MOTIF 43..51
FT /note="'HIGH' region"
FT MOTIF 244..248
FT /note="'KMSKS' region"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 48..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 184
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 196..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 244..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 268..271
FT /note="KIRK -> RLE (in Ref. 1; AAA34809)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..379
FT /note="ADIHKIMGF -> PTFIK (in Ref. 1; AAA34809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 43015 MW; 807B6D21A991E108 CRC64;
MSNKQAVLKL ISKRWISTVQ RADFKLNSEA LHSNATVFSM IQPTGCFHLG NYLGATRVWT
DLCELKQPGQ ELIFGVADLH AITVPKPDGE MFRKFRHEAV ASILAVGVDP EKASVIYQSA
IPQHSELHWL LSTLASMGLL NRMTQWKSKS NIKQSTNGDY LVNDSDVGKV RLGLFSYPVL
QAADILLYKS THVPVGDDQS QHLELTRHLA EKFNKMYKKN FFPKPVTMLA QTKKVLSLST
PEKKMSKSDP NHDSVIFLND EPKAIQKKIR KALTDSISDR FYYDPVERPG VSNLINIVSG
IQRKSIEDVV EDVSRFNNYR DFKDYVSEVI IEELKGPRTE FEKYINEPTY LHSVVESGMR
KAREKAAKNL ADIHKIMGF
