ID   SYV_VIBPA               Reviewed;         952 AA.
AC   Q87LG6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=VP2646;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC60909.1; -; Genomic_DNA.
DR   RefSeq; NP_799025.1; NC_004603.1.
DR   RefSeq; WP_005478852.1; NC_004603.1.
DR   AlphaFoldDB; Q87LG6; -.
DR   SMR; Q87LG6; -.
DR   STRING; 223926.28807656; -.
DR   EnsemblBacteria; BAC60909; BAC60909; BAC60909.
DR   GeneID; 1190191; -.
DR   KEGG; vpa:VP2646; -.
DR   PATRIC; fig|223926.6.peg.2542; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..952
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224593"
FT   COILED          888..952
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   952 AA;  108622 MW;  A6A19D0E6AF0A578 CRC64;
     MEKTYNPTSI EQALYQTWEE KGYFKPHGDT TKESYSIMIP PPNVTGSLHM GHAFQDTIMD
     TLIRCERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKGE
     SGGTITKQLR RLGASVDWDR ERFTMDDGLS NAVQEVFVRL YEDDLIYRGK RLVNWDPKLH
     TAISDLEVEN KDTKGHMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
     RYKDLIGKEI ILPIVDRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHQLPMINI
     LTFDANIRGA AEVFNTNGEP SDAYSTELPA KYHGMERFAA RKAIVAEFDE LGLLEEVKDH
     DLQVPYGDRG GVVIEPMLTD QWYVRTAPLA KTAVEAVENG DIQFVPKQYE NMYFSWMRDV
     QDWCISRQLW WGHRIPAWYD NQGNVYVGRT EEEVRKNNNL ESVIELHQDE DVLDTWFSSA
     LWTFGTQGWP EQTDDLKVFH PSDVLVTGFD IIFFWVARMI MMTMHFVKDE NGKPQVPFKT
     VYVTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVEK RTGNMMQPQL AKKIEKNTRK
     TFENGIEAYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVMMNTEEQD
     CGFNGGEIEY SLADKWIESQ FELAAKAFNN HIDNFRLDMA SNTLYEFIWN QFCDWYLELT
     KPVLWKGTEA QQRGTRRTLI TVLEKTLRLA HPVIPYITET IWQSIKPLVE GVEGETIMLQ
     ALPQFDEANF NQEALDDIEW VKAFITSIRN LRAEYDINPG KPLDVMLKAA NAEDAARLEA
     NKQVLMSLAK LESVRVLAAD EETPACATAL VAKSELMIPM AGLIDKDAEL ARLDGEIKKT
     HGEIKRIEGK LGNEGFVAKA PEAVVAKERE KLEGYKETLA KLEEQKKTIA AL