SYV_BACC1
ID SYV_BACC1 Reviewed; 881 AA.
AC Q72ZW8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BCE_4549;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43450.1; -; Genomic_DNA.
DR RefSeq; WP_000072229.1; NC_003909.8.
DR AlphaFoldDB; Q72ZW8; -.
DR SMR; Q72ZW8; -.
DR EnsemblBacteria; AAS43450; AAS43450; BCE_4549.
DR GeneID; 59154969; -.
DR GeneID; 64199799; -.
DR KEGG; bca:BCE_4549; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002527; 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; -; 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; 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.
FT CHAIN 1..881
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224431"
FT COILED 810..881
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
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 881 AA; 101642 MW; 64305F70DB4FF7DE CRC64;
MSNTEKNLPT KYDHMSVEEG LYQWWLEGKY FEATGDEKKQ PYTIVIPPPN VTGKLHLGHA
WDTTLQDILT RTKRMQGYDV LWLPGMDHAG IATQAKVEGK LREEGISRYD LGREKFLEKA
WEWKEEYASH IRQQWGKVGL GLDYSRERFT LDEGLSDAVN KVFVQLYEKG LIYRGEYIIN
WDPATRTALS DIEVIHKEVQ GAFYHMNYPL TDGSGHIRLA TTRPETMLGD TAVAVHPEDD
RYKHLIGKTV TLPIVGREIP IIADEYVEKD FGTGVVKITP AHDPNDFEVG NRHDLPRILV
MNEDGTMNEK AGKYNGMDRF ECRKALVKDL QEAGVLVEIE PHMHSVGHSE RSGAVVEPYL
STQWFVKMAP LAEKAVALQQ KEEEKVTFVP ERFENTYLRW MENIHDWCIS RQLWWGHRIP
AWYHKETGEV YVGTEAPADI ENWNQDNDVL DTWFSSALWP FSTLGWPNED AADFKRYYST
DALVTGYDII FFWVSRMIFQ GLEFTGERPF KDVLIHGLVR DEQGRKMSKS LGNGIDPMEV
IEKYGADAMR FFLSTGSAPG QDLRFSMEKV ESTWNFINKI WNASRFVLMN MDDMKYEEID
LTGEKSVADK WILTRLNETI ESVTRNMDKY EFGEAGRSLY NFIWDDFCDW YIEMAKLPLY
GEDEAAKKTT RSILAYVLDQ TMRLLHPFMP FVTEKIWQHL PHEGESITVA AWPTVREDLQ
DAEAAAEMHL LVDIIRSVRN IRAEVNTPMS KKVQMQIKAK DEAVLAQLTK NSSYIERFCN
PSELTIQTDL QAPEKAMTAI VTGAELFLPL ADLINLDEER ARLEKELEKF DKEVERVQKK
LSNQGFVAKA PAAVIEGERA KEQDYLEKRE AVRQRLADLE K
