SYV_HELPJ
ID SYV_HELPJ Reviewed; 872 AA.
AC Q9ZK61;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=jhp_1080;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001439; AAD06660.1; -; Genomic_DNA.
DR PIR; E71852; E71852.
DR RefSeq; WP_000807100.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZK61; -.
DR SMR; Q9ZK61; -.
DR STRING; 85963.jhp_1080; -.
DR PRIDE; Q9ZK61; -.
DR EnsemblBacteria; AAD06660; AAD06660; jhp_1080.
DR KEGG; hpj:jhp_1080; -.
DR PATRIC; fig|85963.30.peg.1503; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000804; 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..872
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106228"
FT COILED 810..871
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 531..535
FT /note="'KMSKS' region"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 872 AA; 101166 MW; ECE025361CF0A3EF CRC64;
MKQEPTTYQP EEIEKKIYEI CSHRGYFEIN GNEKIQEKGK RFCLMMPPPN VTGILHIGHA
LTLSLQDILV RYKRMDGYKT LYQPGLDHAG IATQNVVEKQ LLSQGVKKED LGREKFIQKV
WEWKEKSGGA ILEQMKRLGV STAFSRTRFT MDKGLQRAVK LAFLKWYEKG LIVQDNYMVN
WCTKDGALSD IEVEYEERKG ALYYIRYYLE NQKDYLVVAT TRPETLFGDS AIMVNPNDER
YKHLVGQQVI LPLINRTIPI IADAHVEMGF GTGCVKVTPG HDFNDYEVGK RHHLETIKIF
DEKGILNAHC GEFENLERLE ARDKVVAALK ENALLEKIEE HVHQVGHCYR CHNVVEPYVS
KQWFVKPEIA QSSIEKIQQG LARFYPSNWI NNYNAWMREL RPWCISRQLF WGHQIPVFTC
ENNHQFVSLD TPLSCPTCKS EKLEQDKDVL DTWFSSGLWA FSTLGWGQEK SDLFNESDLK
DFYPNTTLIT GFDILFFWVA RMLFCSESLL GELPFKDIYL HALVRDEKGE KMSKSKGNVI
DPLEMIEKYG ADSLRFTLAN LCATGRDIKL STTHLENNKN FANKLFNAAS YLKLKQESFK
DKERLNEYQT ALGRYAKSRL NLVTKEVRNA LDNYRFNDAT TLLYRFLWGE FCDWFIEFSK
VENEAIDELG SVLKEALKLL HPFMPFISES LYHKLSNTEL ENAHSIMVMP YPKEIAQDEK
LEHEFEVIKD CIVSLRRLKI MLETPPIVLK EASVGLREKI ENTERLQNYA QKLAKLEKVS
VITYKPLKSV SDVGEFCQTY ADLENLDLSP LIARLKKQLE KLEKEKLKLN LHNENFVKNA
PKSVLEKARE SLKTLLEKEG KIQQELDLLE QP
