SYV_CLOPE
ID SYV_CLOPE Reviewed; 880 AA.
AC Q8XJ42;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=CPE1919;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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 -!- 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; BA000016; BAB81625.1; -; Genomic_DNA.
DR RefSeq; WP_011010681.1; NC_003366.1.
DR AlphaFoldDB; Q8XJ42; -.
DR SMR; Q8XJ42; -.
DR STRING; 195102.gene:10491188; -.
DR EnsemblBacteria; BAB81625; BAB81625; BAB81625.
DR KEGG; cpe:CPE1919; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000818; 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..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224462"
FT COILED 810..845
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 526..530
FT /note="'KMSKS' region"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 880 AA; 101571 MW; 41E77D356D92D7A8 CRC64;
MDNKNISTTY NPKEFEERLY SNWQEKKYFT PVIDKSKKPY TIIMPPPNIT GKLHLGHALD
NTLQDMLIRF KRMQGYCTLW LPGQDHASIA TEVKVENELL KEGLYKKEMG REAFLEKVWE
WTDEYRERIR EQLKKMGCSA DFTREAFTMD ENLSKAVRHV FVKLYKEGLI YQGNRITNWC
PKCQTALSDA EIEYEEKEGN FWHIKYPVVG SEEFLEIATT RPETLLGDSA VAVNPSDERY
AHLVGKMLKL PLTDREIPVI ADDYVDVEFG TGAVKITPAH DPNDFEVGKR HNLPQIRVMD
DSGVINHLGG KYKGLDRYEA RKQMVADLEE LGLLVKIKPH THNVGTHDRC GTVVEPIISK
QWYVKMQSLA DPAIEVVRNK GTKFVPERFE KTYFNWMENI QDWCISRQLW WGHRIPVFYC
KDCGEIMVEL EDPTKCCKCG SENIEQDKDV LDTWFSSALW PFSTLGWPDR TDDLEFFYPT
STLVTGYDII FFWVARMIFS GIHNMGETPF DTVLIHGIIR DAQGRKMSKS LGNGVDPLEV
IDEYGADALR FMLVTGNAPG NDIRYIPERV EAARNFANKI WNASRFVMMN LDRELMDKYK
DCQEYSLADQ WILSRTNSLI KEVTENMEKY ELGIALQKVH DFLWTEFCDY YIELVKPVLY
GDDEKAKGVV FNVLYTVLNT GLKLLHPVMP FITEEIYTHL STETESITIA TWPTYDEALN
NEKAEKDMTF IMEAIRSLRN LRAEMNVPPS RKAKVMAYAS EEAKDAFING GAYLEKLASA
SEVTFLDNKD NLDNNLVSVV VKGGELFLPL LDLVDREKEL ERLNKEKTKL EGEILRVEKK
LSNERFVSKA PEAVVNEERA KGVKYKEMLE AVLERIEALQ
