SYV_WOLPM
ID SYV_WOLPM Reviewed; 864 AA.
AC Q73HS9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=WD_0464;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; AE017196; AAS14184.1; -; Genomic_DNA.
DR RefSeq; WP_010962612.1; NC_002978.6.
DR AlphaFoldDB; Q73HS9; -.
DR SMR; Q73HS9; -.
DR STRING; 163164.WD_0464; -.
DR EnsemblBacteria; AAS14184; AAS14184; WD_0464.
DR GeneID; 29555025; -.
DR KEGG; wol:WD_0464; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008215; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR InterPro; IPR014070; WPE_wolbac.
DR PANTHER; PTHR11946; PTHR11946; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR TIGRFAMs; TIGR02697; WPE_wolbac; 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..864
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224619"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 589..593
FT /note="'KMSKS' region"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 864 AA; 99846 MW; 0BB0C68AE960398B CRC64;
MLKEKYGFKE VEDKCNILWE GSKVYRWNGE KDNTFTIDTP PPTISGKLHI GHIFSYCHTD
FIARFQRMLG KDVFYPIGFD DNGLPTERLV EQTYKTRAKE VGREKLIEMC HEVIEKSKQE
FKELFKSVGI SYDWDLEYHT ISKETVTLSQ MSFIDLYNKG YAYRKMQPIL WDPVDKTAIA
QAEIEDKVFE SSLNTIVFST EENEQINIAT TRPELLPACV AVFCHPEDAR YTHLIGKTTV
VPITETKVPI IADDKVKIDK GTGLVMCCTF GDELDIYWQQ KHNLPMKIII DQDGRMSLHS
VHGQKEEIWI PVSGHWDDTI GATGMTGERA TQMTKEGGCD QKEEWIPVSA TRMTDDILNE
INGLKVTAAR KRIIEILTEK GLLVESTNIS HSVKCAERSG APLEILPTYQ WFIKTLEQKA
QILDKVKECN WHPSNMRKRM EVWIEGLNWD WCISRQRYFG VPFPAWYSKR KGEEGKIILA
EIKALPIDPS KDLPKGYSKE EIIPDQDVMD TWATSSITPQ LSALAVNSEF SLPNHRYDTI
FPADLRSQSH EIIRTWAFYT ILKAHYHANS LPWKNIMISG WCLADDKKKM SKSKGNIITP
HIILETYGAD VVRYWAANSR LGVDTVYSEN TFKIGKRLVT KLWNASKFVS MFMEKHQVMS
INSAHETMDK WILSKLYKVI ERATNNLLQF EYCEALGAIE EFFWKDFCDS YLELVKKRAY
GSSEATLSAK QSLAYVLNVI LRLFAPFLPY ITEEIYHQLY SYNSVHNQSN WPSKEELIYD
KYSEEMGDNV IQILNIIRKI KADNNVSVKH LIKKLMIKAD LRKDKLDQSA QNDLQAVCNA
ETIEWMQSEL ETEDEKYIVN IDLY
