ID   SYW_METAC               Reviewed;         437 AA.
AC   Q8TUA1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN   Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140};
GN   OrderedLocusNames=MA_0172;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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:0000255|HAMAP-Rule:MF_00140};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00140}.
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DR   EMBL; AE010299; AAM03625.1; -; Genomic_DNA.
DR   RefSeq; WP_011020230.1; NC_003552.1.
DR   AlphaFoldDB; Q8TUA1; -.
DR   SMR; Q8TUA1; -.
DR   STRING; 188937.MA_0172; -.
DR   EnsemblBacteria; AAM03625; AAM03625; MA_0172.
DR   GeneID; 1472064; -.
DR   KEGG; mac:MA_0172; -.
DR   HOGENOM; CLU_032621_3_0_2; -.
DR   InParanoid; Q8TUA1; -.
DR   OrthoDB; 371821at2157; -.
DR   PhylomeDB; Q8TUA1; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
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   HAMAP; MF_00140_A; Trp_tRNA_synth_A; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
DR   PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..437
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136722"
FT   MOTIF           74..82
FT                   /note="'HIGH' region"
FT   MOTIF           321..325
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   437 AA;  49067 MW;  10DF8FBBBFE7A365 CRC64;
     MDTKLDPWSS SDITDYSKLF EEFGISPFEN VLPEIPSPHM YMRRKVIFGH RDYEQIAEAM
     RTGAPFSVMD GFMPSGKVHL GHKMVMDQIV WHQEMGASAF VGIADREAFS VRGFSWQKCR
     EIGVEEYILS LIALGFKPDG LIYFQSGCGS VKDLAFELGA KVNFSELSAI YGFSGETSLS
     HMLSVATQAA DILQPQLEEF GGPKPVVVPV GPDQDPHLRL TRGLAGKMNM FRVEEREDVK
     TGRKYLSVRG KTAQKEALQE LKKRIPGKVK LYEEHIDVLE YPDLAGLEKL VREVTVEFGG
     YAFIPPASTY HRFMSGLQGG KMSSSIPESQ IALTDSPKEG AKKVKRAKTG GCVTLEEQKK
     LGGKPEECSV FELMLFHLIA SDEELLEIKQ ECISGTRMCG SCKQLAAEKM QEFLKDHQEK
     RELAREHLDE YRIIYKD
//