SYW_RALSO
ID SYW_RALSO Reviewed; 400 AA.
AC Q8Y0A1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tryptophan--tRNA ligase;
DE EC=6.1.1.2;
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
GN Name=trpS; OrderedLocusNames=RSc1143; ORFNames=RS04610;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL646052; CAD14845.1; -; Genomic_DNA.
DR RefSeq; WP_011001093.1; NC_003295.1.
DR AlphaFoldDB; Q8Y0A1; -.
DR SMR; Q8Y0A1; -.
DR STRING; 267608.RSc1143; -.
DR EnsemblBacteria; CAD14845; CAD14845; RSc1143.
DR GeneID; 60500656; -.
DR KEGG; rso:RSc1143; -.
DR PATRIC; fig|267608.8.peg.1161; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_0_1_4; -.
DR OMA; GWGQFKP; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF00579; tRNA-synt_1b; 2.
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; Reference proteome.
FT CHAIN 1..400
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136665"
FT REGION 173..241
FT /note="Insert"
FT REGION 280..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..20
FT /note="'HIGH' region"
FT MOTIF 265..269
FT /note="'KMSKS' region"
FT COMPBIAS 280..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 45484 MW; D551F6CE02657DAA CRC64;
MFPERVLSGM RPTGALHLGH YHGVLKNWVR LQAEYPCFFF VADWHALTTH YESPEVIEES
VWEMLIDWLA AGVDPTQATL FIQSRVPEHA ELFLLLSMGT PLGWLERVPT YKDQIEKLKE
KDLSTYGFLG YPLLQAADIL IYRAGFVPVG EDQVPHVEMT REVARRFNYL YGREPGFEQK
ALDAAKKLGG KRAKLYLELR TAHQERGEDD ALEQARALLA ESQSLSMGDR ERLFGYLEGA
RKIILPEPQV LLTEASRMPG LDGQKMSKSY GNTIRMREDK ASVEKKVRTM PTDPARVRRT
DPGDPGKCPV WQLHQVYSDA DTREWVQKGC RSAGIGCLEC KQPVIDGILR EQQPMLERAQ
KYMDDPSLLR AIIADGCDTA HKVTQETMRE VREAMGLTYS