SYW_THEON
ID SYW_THEON Reviewed; 384 AA.
AC B6YUH1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=TON_1666;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ17156.1; -; Genomic_DNA.
DR RefSeq; WP_012572628.1; NC_011529.1.
DR AlphaFoldDB; B6YUH1; -.
DR SMR; B6YUH1; -.
DR STRING; 523850.TON_1666; -.
DR EnsemblBacteria; ACJ17156; ACJ17156; TON_1666.
DR GeneID; 7017335; -.
DR KEGG; ton:TON_1666; -.
DR PATRIC; fig|523850.10.peg.1679; -.
DR eggNOG; arCOG01887; Archaea.
DR HOGENOM; CLU_032621_0_1_2; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 33997at2157; -.
DR Proteomes; UP000002727; 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; 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.
FT CHAIN 1..384
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_1000096114"
FT MOTIF 81..89
FT /note="'HIGH' region"
FT MOTIF 252..256
FT /note="'KMSKS' region"
SQ SEQUENCE 384 AA; 44884 MW; F51516595CC2B64C CRC64;
MDEFKVTPWD VEGLVDYNKL IEEFGTSPLT DELLEKTAQL TKSELPLYFR RRFFFSHRDY
DKVLQDYESG KGFFLYTGRG PSGPMHIGHI IPFFATKWLQ EKFGVNLYIQ ITDDEKFLFK
DKLTFEDTKY WAYQNILDII AVGFDPDRTF IFQDSEFTKI YEMAIPIAKK INFSMAKAVF
GFTEQSKIGM IFYPAIQAAP TFFEKKRCLI PAAIDQDPYW RLQRDFAESL GYYKTAAIHS
KFVPGLMGLE GKMSASKPET AIYLTDDPEE VGRKIWKYAL TGGRATAKEQ REKGGEPEKC
VVFKWLEIFF EEDDKKLMER YHACKNGELL CGQCKRYLIK KVQEFLKEHQ KKRKEAEKKV
EKFKYTGELA REQWDKAVPE ALKG
