SYV_BORPA
ID SYV_BORPA Reviewed; 960 AA.
AC Q7W6P3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, 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=BPP2859;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640431; CAE38151.1; -; Genomic_DNA.
DR RefSeq; WP_010928771.1; NC_002928.3.
DR AlphaFoldDB; Q7W6P3; -.
DR SMR; Q7W6P3; -.
DR EnsemblBacteria; CAE38151; CAE38151; BPP2859.
DR KEGG; bpa:BPP2859; -.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001421; 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.
FT CHAIN 1..960
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224446"
FT COILED 893..955
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 61..71
FT /note="'HIGH' region"
FT MOTIF 569..573
FT /note="'KMSKS' region"
FT BINDING 572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 960 AA; 107268 MW; 71B1D428AF93BE83 CRC64;
MTDAAPNQPV NESQKLSKSF EPAEIETRWY DEWAKRGYFD AGRHVETGTD PQPYVIQFPP
PNVTGTLHMG HAFNQTIMDG LVRYHRMLGD DTVFVPGTDH AGIATQIVVE RQLDAQKVSR
HDLGREKFVE KVWEWKEQSG STITGQVRRL GASADWPREY FTMDARMSRG VAETFVRLYQ
QGLIYRGKRL VNWDPKLLTA VSDLEVQSEE VDGHMWHILY PFVDGPQTIT DQDGNTVTLR
GMTIATTRPE TMLADGALCV HPDDPRYKHL LGKLVELPLC DRNIPIIADD FVDPDFGTGC
VKITGAHDFN DYACALRHDI PLIVIFTLDA HINENGPKQF QGLERYEARQ AVVAELQAQQ
YLVKVEPHKM MQPKGDRTGV VLEPMLTDQW FVAMSKPAPA STLNPGKSIT EVALEAVADG
RIAFYPENWA TIYNQWLNNI QDWCISRQLW WGHQIPAWYS EDGQVFVARS EQEAQEQARA
AGVAGPLTRD PDVLDTWFSS ALVPFTTFGW PEDTPDLRRY LPSSVLVTGF DIIFFWVARM
VMLTMHMTGS VPFKHVYVHG LIRDADGQKM SKSKGNTLDP VDLIDGIDLE GLVRKRTFGL
MNPKQAGAIE KATRRQYPDG IPAFGTDALR FTMAAYATLG RNINFDLKRC EGYRNFCNKL
WNATRFVLMN TEGHALDGDG GELSFADRWI VSQLQALEAE VERGFADYRF DNVANALYRY
VWDEYCDWYL ELAKVQIQQG TPAQQLGTRR TLIRVLEAVL RLAHPVIPFI TEELWQKVAL
VAGKRTAGAV ASVSVQPYPR ANPQAVDAEA EAAVAELKSQ VEAVRALRGE MNLSPAQRVP
LVAEGPTDVL SRNAPYLAAL AKLSEVEVVA ALPDAGAPVQ VVGDARLMLH VEIDVAAECA
RLDKEIARLE GEIAKANGKL GNASFVERAP AAVVEQEKAR LAQFSETLKK VRGQRVKLGA
