ID   SYW_HYPBU               Reviewed;         373 AA.
AC   A2BLD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Hbut_0947;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM80795.1; -; Genomic_DNA.
DR   RefSeq; WP_011822113.1; NC_008818.1.
DR   AlphaFoldDB; A2BLD4; -.
DR   SMR; A2BLD4; -.
DR   STRING; 415426.Hbut_0947; -.
DR   EnsemblBacteria; ABM80795; ABM80795; Hbut_0947.
DR   GeneID; 4782824; -.
DR   KEGG; hbu:Hbut_0947; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_3_0_2; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 33997at2157; -.
DR   Proteomes; UP000002593; 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   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; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..373
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_1000018995"
FT   MOTIF           79..87
FT                   /note="'HIGH' region"
FT   MOTIF           257..261
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   373 AA;  43646 MW;  F351ABD38649A86C CRC64;
     MEGYRLDPWA SAIRLEYEKL FRYFGIKPFQ PLLPEVEKAF GKPHRLMRRG IIFGHRDYEK
     ILEAYRSGER IALVTGFMPS GKFHFGHKMV ADQIIYYQKL GFEIFVVIAD AEAYAVRRLD
     RRKIIEIGLY EYVANLIALG LEKNKHTHIY FQTNYETPYY RLIQMFSRRV TLEEMSAIYG
     DLEPSKIMAA LTQAADILHP QLDYFGGFKY VVVPVGADQD PHIRLTRDIA ARFENELGLR
     RPASTYHRFQ TGLDGNKMSS SRPEYTIFLT DPVDIAVRKL KRALTGGRAT VEEQRRLGGE
     PEKCTVYEFY LYHLIEDDTQ LRKIYEDCRG SRLLCGPDKE YAAELLAKFL EEHQRRLERA
     RDRVLEYVEP PKF