ID   SYV_BACCZ               Reviewed;         881 AA.
AC   Q633Y6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BCE33L4202;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU16067.1; -; Genomic_DNA.
DR   RefSeq; WP_000072217.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q633Y6; -.
DR   SMR; Q633Y6; -.
DR   EnsemblBacteria; AAU16067; AAU16067; BCE33L4202.
DR   KEGG; bcz:BCE33L4202; -.
DR   PATRIC; fig|288681.22.peg.1181; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000002612; 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_0000224433"
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;  101644 MW;  E82EAB502A1C20CA 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
     MNEDGSMNEK AGKYNGMDRF ECRKALVKDL QEAGVLVEIE PHMHSVGHSE RSGAVVEPYL
     STQWFVKMAP LAEKAVALQQ KDEEKVTFVP 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
     DTEAAAEMHL LVDIIRSVRN IRAEVNTPMS KKVQMQIKAK DEAVLAQLTK NSSYIERFCN
     PSELTIQTDL QAPEKAMTAI VTGAELFLPL ADLINLDEER ARLEKELEKF DKEVERVQKK
     LSNQGFVAKA PAAVIEGERA KEQDYLEKRE AVRQRLADLE K