SYW_SULTO
ID SYW_SULTO Reviewed; 381 AA.
AC Q976M1; F9VMM5;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 25-MAY-2022, entry version 102.
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=STK_01690;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAK54171.1; -; Genomic_DNA.
DR RefSeq; WP_010978108.1; NC_003106.2.
DR AlphaFoldDB; Q976M1; -.
DR SMR; Q976M1; -.
DR STRING; 273063.STK_01690; -.
DR EnsemblBacteria; BAK54171; BAK54171; STK_01690.
DR GeneID; 42799641; -.
DR KEGG; sto:STK_01690; -.
DR PATRIC; fig|273063.9.peg.208; -.
DR eggNOG; arCOG01887; Archaea.
DR OMA; SIYHRFM; -.
DR OrthoDB; 33997at2157; -.
DR Proteomes; UP000001015; 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_0000136734"
FT MOTIF 82..90
FT /note="'HIGH' region"
FT MOTIF 254..258
FT /note="'KMSKS' region"
SQ SEQUENCE 381 AA; 44718 MW; 109F5A56AF7D7159 CRC64;
MAQDFNVTPW EVKGKVDYDK LIVQFGTQKI TSELKEKIKS IINDELHVML RRDVFFSHRD
LDLVLKDYQD GKGFFLYTGR APSLGMHIGH LIPFIFTKWL QDKFNVNLYI EITDDEKFMR
NPEYTLDQTR QWAYDNILDI IAVGFNPDKT FIFQDTEYIR NMYPIAIKIA KKLTFSEVRA
TFGLDTSSNI GIIWYPALQI APTMFEKRRC LIPAGIDQDP YWRLQRDIAE SLGYYKAAQI
HSKFLPPLTG PEGKMSSSQP ETAIYLTDDP KTVERKIMKY AFSGGQPTIE LHRKYGGNPD
IDVSFQWLYM FFEPDDNKIK KIEEDYRSGA LLTGELKQIL IEKLNDFLEE HRQKREEAKK
LVNVFKYDGE LAREMWRKIH E