ID   SYW_THEAC               Reviewed;         426 AA.
AC   Q9HIW5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=Ta1211;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445066; CAC12336.1; -; Genomic_DNA.
DR   RefSeq; WP_010901618.1; NC_002578.1.
DR   AlphaFoldDB; Q9HIW5; -.
DR   SMR; Q9HIW5; -.
DR   STRING; 273075.Ta1211; -.
DR   EnsemblBacteria; CAC12336; CAC12336; CAC12336.
DR   GeneID; 1456706; -.
DR   KEGG; tac:Ta1211; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_3_0_2; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   Proteomes; UP000001024; 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; 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; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136735"
FT   MOTIF           66..74
FT                   /note="'HIGH' region"
FT   MOTIF           314..318
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   426 AA;  49200 MW;  CC019B7FC2B5609E CRC64;
     MINPWSSSDF FDYERLKREF GIGDMNVPFD HFLFRRHLIL GQRSIDYIDY ALKHHMKFNV
     MTGLMPSGEM HLGNKSAIDQ VIFFQKLGGR VSIAVADLES YSTRGISLER AREVAIEKYI
     LNYIAMGLEP CEIYFQSRNS DVQFLAYMLG NRTNMSELRS LYGFTDTHDL LHINAPLIQA
     ADVLHTQMKK YGGPAPTVVP VGFDQDPHLR LMRDLAKRMR IFNIQLENDL VVSVRGKDDP
     KEYIDMAYEY LSSRYTNVKK DYEYRVVRAD GVDQQDLVGI DLDLAHMETK YNDFAFIAPS
     ATYQKLMKGL KGGKMSSSVP DSLISLNDDP KEARRKIMAG MTGGRDTEEE QRRLGGEPDR
     CPIFDLYNYE IDDDKHVKEV YDDCRNGKRM CGFCKREIAD RMASWLSDLS KKREEAREKL
     SLYIHE