SYV_MESFL
ID SYV_MESFL Reviewed; 873 AA.
AC Q6F1B1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Mfl355;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE017263; AAT75712.1; -; Genomic_DNA.
DR RefSeq; WP_011183252.1; NC_006055.1.
DR RefSeq; YP_053596.1; NC_006055.1.
DR AlphaFoldDB; Q6F1B1; -.
DR SMR; Q6F1B1; -.
DR STRING; 265311.Mfl355; -.
DR PRIDE; Q6F1B1; -.
DR EnsemblBacteria; AAT75712; AAT75712; Mfl355.
DR GeneID; 2898008; -.
DR KEGG; mfl:Mfl355; -.
DR PATRIC; fig|265311.5.peg.353; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000006647; 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; Reference proteome.
FT CHAIN 1..873
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224503"
FT COILED 804..873
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 873 AA; 102390 MW; 3F37B327E375F385 CRC64;
MKKELEAKYS YEIVEENRYE WWIQNEYFKA NPDSKKPKFS IVLPPPNVTG KLHIGHAWDG
SLQDAIIRFK KLNGFDVLYL PGMDHAGIST QVKVEAKLRE QGISRFELGR EKFLEQAWKW
KHEYAAIIRQ QWSKLGLAFD YSMEKFTLDD DINKIVTEIF VDFYNKGLIY KGKRIVNWDP
MQKTAISNVE VIYKEVEGFM YHFKYMIQGT NEFLNVATTR PETMFADQCL VVNPKDERYT
SFIGKKAINP VNNQAIPIIA DDYVELDFGT GVMKCTPAHD LNDFEIAVRH NLEKPICMNE
DGTINEMGGE EYQGLDRFEA RNKIIENLTK EKTFIKAEPM IHQVGFSERS NAIVEPYLSD
QWFVKMDSFA DMILKLQESN DKIKFFPERF DQVLKKWMEN IHDWTISRQL WWGHRIPAWY
NKEDKTKIYV GMEAPKDAEN WIQDEDVLDT WFSSGLWPFA TLMRGEGFES KYFKEYLPNG
VLVTGHDIIF SWVSRMIFQT IEYTGQIPFK DVLIHGLVRD EHGAKMSKSL GNGIDPMDVI
VNNGSDSLRF SLLTNSTPGQ DIRYSDSKVK AAWNFINKLW NASRYVLMNL EEDFKPWEEQ
AILNSNSLNE TDKWVLTEFS KVSKQVNYLI DKYEFAIAGK MLYDFVWNTY CSWYIEFAKV
NLNNPKTKEA TQQTIVYLLK NILIMLHPYL PFVTEHIYKT LDMKNSILEE SWFDKEFVFE
TDYINVVIEL INSIREFRAT NNIKNNVLLN WNATNGNLEI ITKYNLEINN FLNEFVNANL
SINESLVSET TSLSVLDFFI EIPNDDFIDK EKMLEELATK KKELENEISR SERMLSNENF
ISKAAPSKIE EEKEKYELYK QQLELIQDKL NKM
