SYW_THEVO
ID SYW_THEVO Reviewed; 426 AA.
AC Q978Y8;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=TV1276;
GN ORFNames=TVG1316213;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB60418.1; -; Genomic_DNA.
DR RefSeq; WP_010917511.1; NC_002689.2.
DR AlphaFoldDB; Q978Y8; -.
DR SMR; Q978Y8; -.
DR STRING; 273116.14325515; -.
DR PRIDE; Q978Y8; -.
DR EnsemblBacteria; BAB60418; BAB60418; BAB60418.
DR GeneID; 1441393; -.
DR KEGG; tvo:TVG1316213; -.
DR eggNOG; arCOG01887; Archaea.
DR HOGENOM; CLU_032621_3_0_2; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 33997at2157; -.
DR PhylomeDB; Q978Y8; -.
DR Proteomes; UP000001017; 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; 2.
DR PRINTS; PR01039; TRNASYNTHTRP.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..426
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136736"
FT MOTIF 66..74
FT /note="'HIGH' region"
FT MOTIF 314..318
FT /note="'KMSKS' region"
SQ SEQUENCE 426 AA; 48768 MW; 7884711A187319E2 CRC64;
MINPWSSSDF FDYERLKKEF GISDQSDNID HFLFRRKVIL GQRGFEYIKY AIDNKIKFNV
MTGLMPSGEM HLGNKSAIDQ VIYFQKLGGS VSIAVADLES YSTRGIPLDK AREIAIEKYI
LNYIAMGLQP CEIYFQSKNK DVQFLSYILG NWTNMNELKA LYGFTDSNDI LHINAPLIQA
ADVLHTQLNN YGGPAPTVVP VGFDQDPHIR LMRDLAKRMR IFNVFYDGGI TVSIKGKGDS
TMPVDQAYEY LSKRFSEVTK DYEYRVVKAK DGKEEDIVRT DIDLAKIGSE FNVFSFIPPS
ATYQKLMKGL KGGKMSSSVP DSLISMNDDV EEAKRKIMRA LTGGRDTEEE QRKLGGEPEK
CPVFDLYNYE IDDDKYVNEV FEECKSGKRM CGYCKREIAD KMSIFLKDIK EKREIAREKL
SLYIHE
