ID   SYV_PHOV8               Reviewed;         875 AA.
AC   A6L3G7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BVU_2574;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR40231.1; -; Genomic_DNA.
DR   RefSeq; WP_005848198.1; NC_009614.1.
DR   AlphaFoldDB; A6L3G7; -.
DR   SMR; A6L3G7; -.
DR   STRING; 435590.BVU_2574; -.
DR   EnsemblBacteria; ABR40231; ABR40231; BVU_2574.
DR   KEGG; bvu:BVU_2574; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_10; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; BVUL435590:G1G59-2678-MON; -.
DR   Proteomes; UP000002861; 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; 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..875
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000022164"
FT   COILED          805..875
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           534..538
FT                   /note="'KMSKS' region"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   875 AA;  99754 MW;  33A2896C762D966D CRC64;
     MELASKYNPA DVEGKWYQYW LDNKLFSSKP DGREPYTVVI PPPNVTGVLH MGHMLNNTIQ
     DILVRRARME GKNACWVPGT DHASIATEAK VVNKLAGQGI KKTDLSRDEF LKHAWAWTEE
     HGGIILKQLR KLGASCDWDR TAFTMDEERS ESVIKVFVDL YNKGLIYRGV RMVNWDPKAL
     TALSDEEVIY KEEHSKLYYL RYKVEGDAEG RYAVVATTRP ETIMGDTAMC INPNDPKNQW
     LKGKKVIVPL VNRIIPVIED DYVDIEFGTG CLKVTPAHDV NDYMLGEKYN LPSIDIFNDN
     GTLSEAAGLY VGMDRFDVRK QIEQDLQAAG LLEKVEAYTN KVGFSERTNV AIEPKLSMQW
     FLKMQHFADM ALPPVMNDEL KFYPAKYKNT YKNWLENIKD WCISRQLWWG HRIPAYFLPE
     GGYVVAETAE EALKLAQEKT GNTNLKMEDL RQDDDCLDTW FSSWLWPISL FNGINNPNNE
     EINYYYPTSD LVTGPDIIFF WVARMIMAGY EYKGDMPFKN VYFTGIVRDK LGRKMSKSLG
     NSPDPLELID KYGADGVRMG MMLAAPAGND ILFDDALCEQ GRNFNNKIWN AFRLVKGWEV
     ADIAQPEYAR LATEWFESML AKTAAEVADL FGKYRLSEAL MAVYKLFWDE FSSWYLEMIK
     PAYGQPIDKA TYEKTLGFFD NLLKLLHPFM PFITEELWQH IYDRKEGESL MVQQLNIPTA
     CNEIIVKEFE VVKEVIGGIR TIRLQKNIAQ KETLELQVVG VNPVATFNPV ITKLCNLSSI
     EAVENKADGS GSFMVGTTEY AIPLGNLINT EEELAKLEAD LKYQEGFLQS VLKKLSNEKF
     VSKAPANVID MERKKQADAE SKIASLKESI AALKK