ID   SYV_CLOAB               Reviewed;         881 AA.
AC   Q97GG8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=CA_C2399;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80354.1; -; Genomic_DNA.
DR   PIR; G97195; G97195.
DR   RefSeq; NP_349014.1; NC_003030.1.
DR   RefSeq; WP_010965695.1; NC_003030.1.
DR   AlphaFoldDB; Q97GG8; -.
DR   SMR; Q97GG8; -.
DR   STRING; 272562.CA_C2399; -.
DR   EnsemblBacteria; AAK80354; AAK80354; CA_C2399.
DR   GeneID; 44998879; -.
DR   KEGG; cac:CA_C2399; -.
DR   PATRIC; fig|272562.8.peg.2596; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000814; 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..881
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224461"
FT   COILED          721..747
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   COILED          811..881
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           527..531
FT                   /note="'KMSKS' region"
FT   BINDING         530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   881 AA;  102021 MW;  3ADF33DE57CFAF79 CRC64;
     MKEFDEMAKT YDPKEFEDRI YKWWEEEGFF TPKVDKNKKP YTIMMPPPNI TGKLHLGHAL
     DCALQDFMIR AKRMQGYEAL WLPGQDHASI ATEVRVEKEI LKEGLNKKEM GREKFLERVW
     DWTKEYRERI KGQQKKLGVS ADFTRESFTM DEKLNKAVRT VFVKLYEDGL IYQGNRITNW
     CPKCQTALSD AEIEYKEDQG FFWHIKYPVE GEDSFIEIAT TRPETMLGDT AVAVNPKDER
     YKEFIGKLLV LPLLGRKIPV VADDYVDMEF GTGAVKITPA HDPNDYEVGK RHDLKEIVML
     NNDGTIKEGF GKYSGMDRYE ARKAIVSDLK EEGYLVKIKE HVHNVGTHDR CGNIIEPMVS
     KQWYVKMESL AKPAIEAVKA GKTKFVPERF DKIYFNWMEN IQDWCISRQL WWGHRIPVWY
     CKDCGEIIVS EKEPKACSKC NSENLEQDKD VLDTWFSSAL WPFSTLGWPD KNEDLEYFYP
     TDTLVTGYDI IFFWVARMVF SGIYNMGEVP FKHVYIHGLV RDAEGRKMSK SLGNGVDPLD
     VIDTFGADAL RFMLITGNAP GNDIRYKTEK VEAARNFANK IWNASRFVLM NLDKEIMDKY
     KDLEEYSLAD RWILSRCNSL VREVTDNIEK FELGIASQKV YDFMWNEFCD WYIELVKPVM
     YGEDEKAKGI AYNVLYKVLT VGLQLLHPVM PYITEEIYQH LGGEYKAIAI SAWPTYEEKL
     KNETSENAMN QIIEAIKSIR NVRAEMNVPP SKKAKVMIFT EAENKAAFEM GEHYFEKLAY
     ASSVSFLKSK DEAPENAVSS VTKGAELFMP LLDLIDVTKE IERLSKEKDK LKAEIQRVDK
     KLSNKGFVDK APESVVEAER VKGEKYKKML EAVEERIAAL K