ID   SYV_WIGBR               Reviewed;         881 AA.
AC   Q8D294;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=WIGBR4600;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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   -!- 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; BA000021; BAC24606.1; -; Genomic_DNA.
DR   RefSeq; WP_011070264.1; NC_004344.2.
DR   AlphaFoldDB; Q8D294; -.
DR   SMR; Q8D294; -.
DR   STRING; 36870.25166416; -.
DR   EnsemblBacteria; BAC24606; BAC24606; BAC24606.
DR   KEGG; wbr:valS; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000562; 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   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; IPR009080; tRNAsynth_Ia_anticodon-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   PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..881
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224596"
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   881 AA;  104544 MW;  4C2897194995468F CRC64;
     MKNPYDSKKI ESYFFMFWKK NNLFKKKLNS NKDNFCIILP PPNITGDLHV GHAFQQSIID
     IFIRYNYMKG NNVLLQSGID HAGISTQSIL EKKIYFYENK NRFDYGRKNF IKEIWKWKEE
     SEKKICYQIN KLGCFTDLNK IRFTMDKDSC KAVNNVFLKL YKDKLIYKKK KLMHWDVKLR
     TVISDLEIEN REINGKLWYI KYFFSENSNK NSKLNFLEIA TTRPETIFGD VAVAVNPLDA
     RYNNLIGKYI KVPLTNRSIP IIQDDYVKMD YGSGCVKITP GHDFNDFSIC KNHKLNIINI
     LTISGKICKK PKVYDFNGNS VSDTNIKIPK ELQGLSISEA RNNIVYKLNR KEYITKFEYK
     KVVLPFGDRS GDILEPMLTN QWYIKTKKLS EVAIEAVKEK KIKFISKQYE NMYFGWMENI
     KDWCISRQLW WGHRIPIWYD VNKNQYPGIS ESDVRDNFKI NKEEILTQEE DVLDTWFSSA
     IWSFASLGWP QKSIKFDTFH PTNLIISGFD IIYFWISRMI MLTMYIIKDS FGNPQIPFKN
     IFITGLIRDK NGIKMSKSKG NVIDPIDIID GISLEDLIKK RTKEISNIKL IKKIEKITKK
     EFPNGIQNHG ADAVRLSMAS ISCSNRKINI DIKKIIGYKN FCNKLWNVSK FIIINLKNKK
     VSFEEKEINL HKIDNWILHK YNKVFKYYKY NIDNFRLDLV VNILYEFIWH QFCDWYIENS
     KIIFKNNIIS RLNNTCYTLF FILENSLKML HPFIPFITEE IWKNLSKMVR NERKNTTILE
     FFPKKYLFLK KDNSFNEIEC IKNIITCIRK LKFEKKTKFN KLVDVCFINN SYEEKIIILN
     NIEIIKNIAF VKNVDFSRSI PKNVLKKDIK IINNIKIYIY N