SYV_MESH2
ID SYV_MESH2 Reviewed; 822 AA.
AC Q5ZZL4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=mhp694;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(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; AE017332; AAV27679.1; -; Genomic_DNA.
DR RefSeq; WP_011206524.1; NC_006360.1.
DR AlphaFoldDB; Q5ZZL4; -.
DR SMR; Q5ZZL4; -.
DR STRING; 295358.mhp694; -.
DR EnsemblBacteria; AAV27679; AAV27679; mhp694.
DR KEGG; mhy:mhp694; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q5ZZL4; -.
DR Proteomes; UP000006822; 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; 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; 2.
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..822
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224508"
FT COILED 765..822
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 511..515
FT /note="'KMSKS' region"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 822 AA; 97252 MW; BC00782DE5E83405 CRC64;
MKNKYDFKLV EEKRNEKWQK KGFFIAPKQT KKPFSIISPP PNVTGQLHLG HSWNAFIQDS
LVRYHKLQGF DVLLLPSVDH AGIATQVKVE EDLAKKGIKK SDLKREEFIK KCYHWKEKQY
LKIKEQWDKL GICYDFSKER FTLDQDAQIA VSDFFIKLWE KNLIYRGQKA INWDIKLQTA
ISNIEVINKP VEQKMYYLKY FLENSNEFLT VATTRIETIS SDVALAINPK DKRYLHLVGK
KVVHPLTKKL IKIIADSNVG SDFGSGIMKV SAHSILDFEI MEKHNLESKD CIDNYGNLNH
EVPEFQGQNR FFARDLIAKK LEKEGFLAKI ETVISNVGFS QRSDEIVEIL KKPQWFVKMD
ELAKSLISHL NSKDKIKFYP KNFEKNLRKW FEKIHDWTIS RQLWWGHRIP VWYKNDEFKV
QIDSPGQGWI QDEDVLDTWF SSGISVFAFL GWPQNFDLIK SYFPTSLLVT GWDILFFWVA
RMYFSSLFIM KQKPFEKVLL HGLIRDEIGR KMSKSLGNGL DPMEIIEKYG SDTLRQALIF
NSSPGKDIKF NIEKLNTAWN LNNKIWNIAK YIADLDTFFA KPDLIDLWME NKIYILKRQI
VKNIKKYNFS VIGTEINNFI YGDFSSRYIE LIKTRKNGFY ARKLLRKVLI ILHPFLPFLT
DFLMEKIFKM EILEQKMPRI RQFKENQKVE NILEIIDNLR TYREKFQISK KIILEYCIIN
DKFSNAEIDI INKLTFGKWL ENKELVIKTK NFEIAIKVPE ELKKEQKGRE LKEIQFLKSE
ILRAEKILTN KGFLEKAPRE KIDLERTKLE KLKEKLAFYE KK
