SYV_WOLSU
ID SYV_WOLSU Reviewed; 894 AA.
AC Q7M8H7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=WS1652;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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; BX571661; CAE10683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7M8H7; -.
DR SMR; Q7M8H7; -.
DR STRING; 273121.WS1652; -.
DR PRIDE; Q7M8H7; -.
DR EnsemblBacteria; CAE10683; CAE10683; WS1652.
DR KEGG; wsu:WS1652; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000422; 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; Reference proteome.
FT CHAIN 1..894
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224597"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 832..894
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 894 AA; 102730 MW; DA2CACBC57FEA8EB CRC64;
MKSIQTPSKS HTNTKETPVM SQEETKGYNP REIEESYYKI WETRGYFEVE GNAQIQKPNQ
NFAVMLPPPN VTGSLHIGHA LNHTLIDIMT RYKRMDGYKT LWQPGTDHAG IATQNVVEKR
LLSKGIKKEE LGREAFLEKV WEWREESGGT ILSQMRKLGT SPAWSRTRFT MDEGLKNSVA
RAFVKLYEEG YIIRGNYMVN WCTHDGALSD IEVEYDANKG KLYHLRYFFK DSSDYIVVAT
TRPETFFGDT AVMVHPEDER YAHLIGQTLV LPLIGREIQI IADSYVDREF GTGMVKVTPA
HDPNDYEVGK RHDLEFITVF DKEGYLNHHA GEFEGLERLE AREAIVAKLQ EKGYIEKIEE
HENQVGKCYR CGNVVEPYIS KQWFVKKEVA QKAIERINSG EAAFYPAQWK NNYNAWMKEL
RDWCISRQLW WGHQIPVYYC DCGHEWASET TPSHCPKCQG SQFHQDPDVL DTWFSSALWP
FSTLGWGNGE AGKGSWWREE DLQEFYPNSL LITGFDILFF WVARMLMMGE HFLDNLPFKD
IYLHALVRDE KGQKMSKSKG NVIDPLELIE KYGCDSTRFT LAILCAQGRD VRLSSQQLEI
SKNFTNKLYN AANFLLLNAS SFKTLDEITP QTPLGRYMAS RFSLCVEELR GALDGYRFND
GATVLYRFLW GEFCDWGIEL SKANKEAINE LGAIFREAMK LLHPYMPFIS EHLYQKLGGA
RLEESTSIMI LPYPKANWRE EKIEMTFEVI MDAIISTRRL KATLELANQK IPVVFIKAPQ
GMDESLINTF IPRLAKVDSI ELLSEKPAAC VVDVGEKCEI YLSTAQLDLS PIISRLEKQQ
EKLQKEVDKL LGMLNNEKFV ANAPQNVLEQ NRVALKEAQT KLDKVKVELQ GIKG
