ID   SYV_CORDI               Reviewed;         919 AA.
AC   Q6NFV0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=DIP1786;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248359; CAE50316.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6NFV0; -.
DR   SMR; Q6NFV0; -.
DR   STRING; 257309.DIP1786; -.
DR   EnsemblBacteria; CAE50316; CAE50316; DIP1786.
DR   KEGG; cdi:DIP1786; -.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000002198; 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   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..919
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224465"
FT   COILED          852..919
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           66..76
FT                   /note="'HIGH' region"
FT   MOTIF           562..566
FT                   /note="'KMSKS' region"
FT   BINDING         565
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   919 AA;  103151 MW;  55FB4BC9D108F355 CRC64;
     MVGSRSASHQ KTVKIVPMTN RADKLPKSWD PQAVEKDLYE GWVEKGYFTA DPSSSKPAFS
     IVLPPPNVTG QLHMGHALDH TLMDGIARRK RMQGYEVLWL PGMDHAGIAT QTKVEAMLKE
     TEGKSRWDYS REEFIEHVWE WKRKFGGTIG TQMRAIGDSV DWSRERFTLD EGLSRAVQTI
     FKQMYDRGMI YQANRLVNWS PILETAVSDI EVVYKDVEGE LVSIRYGSLN DDEPHVIVAT
     TRVETMLGDV AVAVHPDDER YADLVGTTLP HPFLPDRQMI VVADDYVDPE FGTGAVKITP
     AHDPNDYALG LRHNLDMPNI MDATGHIAGT GTQFDGMDRF EARVKIREAL AEQGRIVKEV
     RPYVHSVGHS ERSGEPIEPR LSLQWWVKVE KLATMAGDAI REGDTVIHPK SSEPRYFDWV
     DDMHDWCISR QLWWGHRIPI WYGPEDAEGN RDIVCVGPDE QPPAGYEQDP DVLDTWFSSA
     LWPFSTMGWP DKTPELDKFY PTSVLVTAYD ILFFWVARMM MFGTLAGETT PEILGQGTDG
     RPQIPFNDLF LHGLVRDEQG RKMSKSLGNG IDPMDWVERF GADALRFTLA RGANPGVDLP
     VGEDSAQSSR NFATKLFNAT KFALMNGAEV GTLPERSELT DADRWILDRL EEVRVSVDDY
     FDRYQFAKGN EALYQFAWGE FCDWYLEIAK VQIPRDMEAA SAQEQARGRN TQIVLGQVLD
     ALLRMLHPAM PFVTEVLWKA LTDGESLNVA EWPTAAMTNG GVATDEVAAR RMADVEKLVT
     EIRRFRSDQG VKPSQKVPGA VDFAAADLAA QEDLVRSLAR LDQPAEDFAA SASIEVRLSQ
     ATIEISVDTS GTVDKEAERK RLDKDLAAAT KELETTAKKL GNESFLAKAP EAVVAKIRER
     QQIAQEEVAR ISARLEELK