ID   SYW_SULAC               Reviewed;         381 AA.
AC   Q4JBG7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Saci_0450;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(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; CP000077; AAY79862.1; -; Genomic_DNA.
DR   RefSeq; WP_011277364.1; NC_007181.1.
DR   AlphaFoldDB; Q4JBG7; -.
DR   SMR; Q4JBG7; -.
DR   STRING; 330779.Saci_0450; -.
DR   PRIDE; Q4JBG7; -.
DR   EnsemblBacteria; AAY79862; AAY79862; Saci_0450.
DR   GeneID; 3474542; -.
DR   KEGG; sai:Saci_0450; -.
DR   PATRIC; fig|330779.12.peg.448; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_0_1_2; -.
DR   OMA; SIYHRFM; -.
DR   Proteomes; UP000001018; 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; 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..381
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136732"
FT   MOTIF           82..90
FT                   /note="'HIGH' region"
FT   MOTIF           254..258
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   381 AA;  44604 MW;  AB6DCEFB7638A3D0 CRC64;
     MAQDFTVTPW EVKGKVDYDK LIVQFGTQKM TSELKERAKR AINDELHVML RRDVFFSHRD
     FDLILNDYEK GNGFFLYTGR APSLGMHIGH LIPFIFTKWL QEKFKVNVYI EITDDEKFLR
     NVDYTLDQTK EWSYENILDI IAVGFDPNKT FIFQDTEYIK NMYPLSVKIA KKLTFNEVRA
     TFGLDTSSNI GIIFYPALQI VPTMFEKRRC LIPAGIDQDP YWRLQRDIAE SLGYFKAAQI
     HSKFLPPLTG PEGKMSSSQP ETAIYLTDDP KTVERKIMKY AFSGGQATVE LHRKYGGNPD
     IDVAFQWLYM FFEPDDQRIR KIEEDYRSGA MLTGELKQIL VDKLNAFLEE HREKREKAKD
     LVNVFKFDGD LARDMWKRIH V