SYV_HELPY
ID SYV_HELPY Reviewed; 874 AA.
AC P56000;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=HP_1153;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08195.1; -; Genomic_DNA.
DR PIR; A64664; A64664.
DR RefSeq; NP_207944.1; NC_000915.1.
DR RefSeq; WP_000605522.1; NC_018939.1.
DR AlphaFoldDB; P56000; -.
DR SMR; P56000; -.
DR STRING; 85962.C694_05955; -.
DR PaxDb; P56000; -.
DR EnsemblBacteria; AAD08195; AAD08195; HP_1153.
DR KEGG; hpy:HP_1153; -.
DR PATRIC; fig|85962.8.peg.1207; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR PhylomeDB; P56000; -.
DR Proteomes; UP000000429; 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; -; 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; Reference proteome.
FT CHAIN 1..874
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106227"
FT COILED 813..873
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 51..61
FT /note="'HIGH' region"
FT MOTIF 533..537
FT /note="'KMSKS' region"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 874 AA; 101360 MW; BB5668E2ACD5AD28 CRC64;
MIMKQEPTTY QPEEIEKKIY EICSHRGYFE IDGNEAIQEK NKRFCLMMPP PNVTGVLHIG
HALTLSLQDI LARYKRMDGY KTLYQPGLDH AGIATQNVVE KQLLSQGIKK EDLGREEFIK
KVWEWKEKSG GAILEQMKRL GVSAAFSRTR FTMDKGLQRA VKLAFLKWYE KGLIIQDNYM
VNWCTKDGAL SDIEVEYEER KGALYYIRYY LENQKDYLVV ATTRPETLFG DSALMVNPND
ERYKHLVGQK AILPLIHRTI PIIADEHVEM EFGTGCVKVT PGHDFNDYEV GKRHHLETIK
IFDEKGILNA HCGEFENLER LEARDKVVER LKENALLEKI EEHTHQVGHC YRCHNVVEPY
VSKQWFVKPE IAQSSIEKIQ QGLARFYPSN WINNYNAWMR ELRPWCISRQ LFWGHQIPVF
TCENNHQFVS LDTPLSCPTC KSETLEQDKD VLDTWFSSGL WAFSTLGWGQ EKSGLFNESD
LKDFYPNTTL ITGFDILFFW VARMLFCSES LLGELPFKDI YLHALVRDEK GEKMSKSKGN
VIDPLEMIEK YGADSLRFTL ANLCATGRDI KLSTTHLENN KNFANKLFNA ASYLKLKQES
FKDKERLNEY QTPLGRYAKS RLNSATKEAR NALDNYRFND ATTLLYRFLW GEFCDWFIEF
SKVENEAIDE LGSVLKEALK LLHPFMPFIS ESLYHKLSNT ELENTESIMV MPYPKDLAQD
EKLEHEFEVI KDCIVSLRRL KIMLETPPIV LKEASVGLRE AIENTERLQT YAQKLARLEK
VSVISSKPLK SVSDVGEFCQ TYANLENLDL SPLVARLKKQ LEKLEKEKLK LNLHNENFVK
NAPKSVLEKA KESLKTLLEK ESKIKQELDL LEQP
