ID   SYW_THEKO               Reviewed;         384 AA.
AC   Q5JEP3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=TK1874;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD86063.1; -; Genomic_DNA.
DR   RefSeq; WP_011250825.1; NC_006624.1.
DR   AlphaFoldDB; Q5JEP3; -.
DR   SMR; Q5JEP3; -.
DR   STRING; 69014.TK1874; -.
DR   PRIDE; Q5JEP3; -.
DR   EnsemblBacteria; BAD86063; BAD86063; TK1874.
DR   GeneID; 3235830; -.
DR   KEGG; tko:TK1874; -.
DR   PATRIC; fig|69014.16.peg.1832; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   InParanoid; Q5JEP3; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   PhylomeDB; Q5JEP3; -.
DR   Proteomes; UP000000536; 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; -; 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_0000136731"
FT   MOTIF           81..89
FT                   /note="'HIGH' region"
FT   MOTIF           252..256
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   384 AA;  44844 MW;  6C7FD1CF5263DCB2 CRC64;
     MDDFKVTPWD VEGVVDYNKL IEQFGTSPLT DELIEKTAEL TKSELPLFFR RRFFFSHRDY
     DKVLADYESG RGFFLYTGRG PSGPMHIGHI IPFFATKWLQ ENFDVNLYIQ ITDDEKFLFK
     EKLSFEDTKR WAYENILDII AVGFDPDKTF IFQNSEFTKI YEMALPIAKK INFSMARAVF
     GFNEQSKIGM IFYPAIQAAP TFFEKKRCLI PAAIDQDPYW RLQRDFAESL GYYKTAAIHS
     KFVPGLTSLE GKMSASKPET AVYLTDDPEE AGKKIWKFAL TGGQPTLKEQ REKGGNPEKC
     VVFKWFEIFF EPDDEKLMER YRACKAGELT CGQCKRELIE RVQKFLKEHQ KKRKEAEKKV
     EKFKYTGELA QEQWDKAIPE PLRT