ID   SYW_PYRAE               Reviewed;         375 AA.
AC   Q8ZTU5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=PAE3091;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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; AE009441; AAL64664.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTU5; -.
DR   SMR; Q8ZTU5; -.
DR   STRING; 178306.PAE3091; -.
DR   EnsemblBacteria; AAL64664; AAL64664; PAE3091.
DR   KEGG; pai:PAE3091; -.
DR   PATRIC; fig|178306.9.peg.2323; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   InParanoid; Q8ZTU5; -.
DR   OMA; SIYHRFM; -.
DR   Proteomes; UP000002439; 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..375
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136728"
FT   MOTIF           81..89
FT                   /note="'HIGH' region"
FT   MOTIF           258..262
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   375 AA;  43179 MW;  3DDBF85DA680F116 CRC64;
     MEEEFVVTPW EVRGRVDYEK LLKHFGAKPL TKDEVALLEK YAGEVHPLIR RGFFYAHRDF
     DFIMKWHGEG RPWALYTGRG PSGPVHIGHM VPWILLKWFS DKFGLEVYFQ ITDDEKFYDD
     PEMKLEEATN WAYENALDVI ALGFSPERLH LIIDTKDIKP LYPIAVRVAK KLTWNTVKAT
     FGFTDSTNIG LIFYPSLQIA VAFLPTELRR EATPVLIPCA IDQDPYFRLA RDIADALGYP
     KPSTLYSKFI MALTGESKMS ASNPDSAIYT LDDEKTVRRK VMNAFTGGRP TAEEQRKYGG
     NPEVCPVFHY HMLFDPDDAS VEKIRQDCKS GALLCGECKL KLHEKITKFL KEHRERREKA
     RGKVDEYRLS VKLSK