SYV_XYLFM
ID SYV_XYLFM Reviewed; 991 AA.
AC B0U1L1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004};
GN OrderedLocusNames=Xfasm12_0110;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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_02004}.
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_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; CP000941; ACA11149.1; -; Genomic_DNA.
DR RefSeq; WP_004085524.1; NC_010513.1.
DR AlphaFoldDB; B0U1L1; -.
DR SMR; B0U1L1; -.
DR KEGG; xfm:Xfasm12_0110; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 2.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..991
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189250"
FT REGION 689..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 925..988
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 582..586
FT /note="'KMSKS' region"
FT COMPBIAS 689..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 991 AA; 111635 MW; AFD234E55B073F1D CRC64;
MSQFTSSYDP TSFEARLYAE WEAAGHFKPS GTGQPYTILL PPPNVTGTLH MGHAFQQTLM
DALVRYHRMC GDDTLWQVGT DHAGIATEMV VSRNVMLEGR GETRDSLGRD GFINKVWEWK
QQSGDTIERQ MRRLGVSADW SRSTFTMDPQ PSAAVTEAFV RWYEEGLIYR GQRLVNWDPV
LKTAISDLEV ENVAEEGMLW SIRYPLSDGV TYEHIEHDAA GNEILRETRD SLIVATTRPE
TLLGDTAVMV HPEDRRYTAL IGKTVTLPLT GRQVEVISDT CVDPTFGSGV VKVTPAHDFN
DFEVGVRHQL PMIKVLDDAA CILSETYAQG WMTPLNNPKG DSRWINIIDI PESEFVIPAH
LAGLDRYEAR KQILADLDTQ GLLVAAIPHT LQVPRGDRTG QVIEPYLTAQ WFVRMDRLAA
RGLELVERGA VRFVPPNWIN TYRHWMNNIR DWCISRQLWW GHRIPAWFDE YDGSFYVGRS
EAEVRAKHAL GPEVTLTQDS NVLETWFSSQ LWPFSTLGWP DPTAMAERGF ERYLPSSVLV
TGFDIIFFWV ARMIMATDHF TGNVPFHDVY ITGLIRDAQG QKMSKSKGNV LDPLDIIDGI
TLDDLVAKRT TGLMQPKLAE KIAKATRKEF PDGIAPHGAD ALRFTIAALA THGRDIKFDL
GRAEGYKNFC NKLWNATRFV LMNTADDTAH SPAQHQAGQD GQDAPRTPQP RTDAEQWILS
RLAAVTAEAH AQFAAYRFDL LAQALYEFAW NEFCDWFVEL AKPALNGNDT QAAASTRHTL
LYVLETLLRL LHPLIPFITE ELWRQVAPRL GIQATTLMLR PYPQPQQLET AAFANAAADV
EWLKIMVSAL RRIRSTLNVP PSRRISLLLQ GGQEVDRHRI THFAIALHFL LKLEHIDWLS
AATAAPPSAI AIVGSLKLLV PLEGLIDVDA ERARLDKEIK RVESEIDKSN GKLSNAVFVQ
NAPTAVVEQE RSRLTEWTTQ LNGLRERRTT L
