ID   SYV_YERPE               Reviewed;         965 AA.
AC   Q8ZBH1; Q0WBK4; Q74X23; Q7CKF5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
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};
GN   OrderedLocusNames=YPO3443, y0743, YP_0641;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(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; AL590842; CAL22032.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM84330.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS60909.1; -; Genomic_DNA.
DR   PIR; AE0418; AE0418.
DR   RefSeq; WP_002209307.1; NZ_WUCM01000023.1.
DR   RefSeq; YP_002348334.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZBH1; -.
DR   SMR; Q8ZBH1; -.
DR   IntAct; Q8ZBH1; 1.
DR   STRING; 214092.YPO3443; -.
DR   PaxDb; Q8ZBH1; -.
DR   DNASU; 1145690; -.
DR   EnsemblBacteria; AAM84330; AAM84330; y0743.
DR   EnsemblBacteria; AAS60909; AAS60909; YP_0641.
DR   GeneID; 57975266; -.
DR   KEGG; ype:YPO3443; -.
DR   KEGG; ypk:y0743; -.
DR   KEGG; ypm:YP_0641; -.
DR   PATRIC; fig|214092.21.peg.3932; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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; -; 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..965
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224603"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          896..965
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           568..572
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         571
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   965 AA;  109566 MW;  67FD177AA82E8513 CRC64;
     MENTPSHINK TEPSLDKTYS PQEIEQPLYE HWEKQGYFKP NGDTSKESYC IMIPPPNVTG
     SLHMGHAFQQ TIMDTLIRYQ RMQGKNTLWQ AGTDHAGIAT QMVVERKIAA EEGKTRHDYG
     RDAFIDKIWE WKGESGGTIT RQMRRLGNSV DWERERFTMD EGLSNAVKEV FVRLHKEDLI
     YRGKRLVNWD PKLRTAISDL EVENRESKGS MWHLRYPLAD GAKTAEGKDY LVVATTRPET
     VLGDTGVAVN PEDPRYKDLI GKEVILPLVG RRIPILGDEH ADMEKGTGCV KITPAHDFND
     YEVGKRHALP MINILTFDGD IRSEAEVFDT HGEATDAFSN AIPAQFQGLE RFAARKAVVA
     EFEKLGLLEE VKPHDLTVPY GDRGGVVIEP MLTDQWYVHT APLAKVAIEA VENGEIQFVP
     KQYENMYYSW MRDIQDWCIS RQLWWGHRIP AWYDEQGNVY VGRDEAEVRR DNNLGAEVAL
     RQDEDVLDTW FSSGLWTFST LGWPEQTDAL KTFHPTSVVV SGFDIIFFWI ARMIMLTMHF
     MKDENGKPQV PFKTVYMTGL IRDDEGQKMS KSKGNVIDPL DMVDGISLEA LLEKRTGNMM
     QPQLAEKIRK RTEKQFPNGI EPHGTDALRF TLAALASTGR DINWDMKRLE GYRNFCNKLW
     NASRFVLMNT EGQDCGQNGG EMVLSLADRW ILAEFNQTIK AYREAMDTYR FDLAAGILYE
     FTWNQFCDWY LELTKPVMNS GSEAELRGTR HTLIQVLEAL LRLAHPIIPY ITETIWQRVK
     NLKGITADTI MLQPFPEYDA SQVDEQALSD LEWIKQTIIA VRNIRAEMNI APGKPLEVML
     RGANAQAQRR VLENQSFIQS LARLSSLTLL AEGDKGPVSV TKLVEGAEVL IPMAGLIDKA
     TELDRLAKEV AKLDAEIERI EGKLGNEGFV ARAPEAVVAK ERERLAACAE AKQKLIEQQA
     TIAAL