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SYW_THESM
ID   SYW_THESM               Reviewed;         384 AA.
AC   C6A032;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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}; OrderedLocusNames=TSIB_1964;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS91013.1; -; Genomic_DNA.
DR   RefSeq; WP_015850229.1; NC_012883.1.
DR   AlphaFoldDB; C6A032; -.
DR   SMR; C6A032; -.
DR   STRING; 604354.TSIB_1964; -.
DR   EnsemblBacteria; ACS91013; ACS91013; TSIB_1964.
DR   GeneID; 8096977; -.
DR   KEGG; tsi:TSIB_1964; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   Proteomes; UP000009079; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_A; Trp_tRNA_synth_A; 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   InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..384
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_1000203257"
FT   MOTIF           81..89
FT                   /note="'HIGH' region"
FT   MOTIF           252..256
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   384 AA;  44610 MW;  5EE79B3DAC942C65 CRC64;
     MPEFEVTPWE VTGVVDYNKL IEEFGTTPLT DDLLKKTEEL TKKELPMYFK RKFFFSHRDY
     DLVLKDYEAG KGFFLYTGRG PSGPMHIGHI IPFFATKWLQ ENFGVNLYVQ ITDDEKFLFK
     PQLTFEGTKR WAYENILDII AVGFDPDKTF IFQDSEFTKI YEMAIPIAKK VTYSMAKAVF
     GFNEQSKIGM IFFPAIQAAP TFFEEKRSLI PAAIDQDPYW RIQRDFAESL GYYKTAALHS
     KFVPGLMGLG GKMSASKPET AIYLTDDPEE AGKKIWKYAL TGGRATAKEQ RELGGEPDKC
     VVFKWLEIFF EPDEKKLLER YIACKNGEIL CGQCKRYLIE KVQNFLKEHQ EKREKAKKEI
     EKFKYTGDLA REQWDKAIPE PLRK
 
 
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