SYV_VIBVY
ID SYV_VIBVY Reviewed; 951 AA.
AC Q7MHG1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=VV2910;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95674.1; -; Genomic_DNA.
DR RefSeq; WP_011079431.1; NC_005139.1.
DR AlphaFoldDB; Q7MHG1; -.
DR SMR; Q7MHG1; -.
DR STRING; 672.VV93_v1c26340; -.
DR EnsemblBacteria; BAC95674; BAC95674; BAC95674.
DR KEGG; vvy:VV2910; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002675; Chromosome I.
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; -; 1.
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; Reference proteome.
FT CHAIN 1..951
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224595"
FT COILED 882..951
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 951 AA; 108485 MW; 538D0C2697E9B2CF CRC64;
MEKTYNPTSI EQDLYKTWEE QGYFKPHGDT SKESYSIMIP PPNVTGSLHM GHAFQDTIMD
TLIRCERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGREAF IDKIWEWKGE
SGGTITKQLR RLGASVDWDR ERFTMDDGLS NAVQEVFVRL YEDDLIYRGK RLVNWDPKLH
TAISDLEVEN KDTKGHMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
RYQDLIGKDI ILPIVDRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHQLPMINI
LTFDANIRDA AEVFTTNGEP SDAYGTELPA KYHGMERFAA RKAIVAEFDE LGLLEEVKDH
DLQVPYGDRG GVVIEPMLTD QWYVRTAPLA KTAVEAVENG DIQFVPKQYE NMYFSWMRDV
QDWCISRQLW WGHRIPAWYD NQGNVYVGRS EEEVRQNHNL ESVIELHQDE DVLDTWFSSA
LWTFGTQGWP EQTDDLKVFH PSDVLVTGFD IIFFWVARMI MMTMHFVKDE NGKPQVPFKT
VYVTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVEK RTGNMMQPQL AAKIEKNTRK
TFENGIEAYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVMMNTEEQD
CGFGAGEIEY SLADKWIESQ FELAAKAFNN HIDNYRLDMA ANTLYEFIWN QFCDWYLELT
KPVLWKGTEA QQRGTRRTLI TVLEKTLRLA HPVIPYITET IWQSIKPLVD GVEGETIMLQ
SLPQYDEANF NQEALDDIEW VKAFITSIRN LRAEYDINPG KPLEVMLKAD EKDAARLEAN
KQVLMSLAKL ESVRVLAAGE ETPACATALV AKSELMIPMA GLIDKDAELA RLDKEVAKTQ
GEIKRIEGKL GNEGFVAKAP EAVIAKEREK LEGYQETLAK LEEQKATIAA L
