SYV_YERPS
ID SYV_YERPS Reviewed; 965 AA.
AC Q66F11;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, 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=YPTB0529;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH19769.1; -; Genomic_DNA.
DR RefSeq; WP_011191653.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66F11; -.
DR SMR; Q66F11; -.
DR EnsemblBacteria; CAH19769; CAH19769; YPTB0529.
DR GeneID; 66843053; -.
DR KEGG; ypo:BZ17_2033; -.
DR KEGG; yps:YPTB0529; -.
DR PATRIC; fig|273123.14.peg.2159; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001011; 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; -; 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.
FT CHAIN 1..965
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224604"
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; 109585 MW; A623883B722E82FB 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 MLTDQWYVRT 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
