SYV_BACFR
ID SYV_BACFR Reviewed; 876 AA.
AC Q64XH6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-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=BF1050;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD47800.1; -; Genomic_DNA.
DR RefSeq; WP_005801208.1; NZ_UYXF01000020.1.
DR RefSeq; YP_098334.1; NC_006347.1.
DR AlphaFoldDB; Q64XH6; -.
DR SMR; Q64XH6; -.
DR STRING; 295405.BF1050; -.
DR EnsemblBacteria; BAD47800; BAD47800; BF1050.
DR GeneID; 66329975; -.
DR KEGG; bfr:BF1050; -.
DR PATRIC; fig|295405.11.peg.1042; -.
DR HOGENOM; CLU_001493_0_2_10; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002197; 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; -; 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.
FT CHAIN 1..876
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224437"
FT COILED 805..826
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 853..875
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 532..536
FT /note="'KMSKS' region"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 876 AA; 99674 MW; 5611B1DFFACDB487 CRC64;
MELASKYNPA DVEGKWYQYW LDHKLFSSKP DGREPYTIVI PPPNVTGVLH MGHMLNNTIQ
DILVRRARME GKNACWVPGT DHASIATEAK VVNKLAAQGI KKTDLSRDEF LKHAWAWTDE
HGGIILKQLR KLGASCDWDR TAFTMDEKRS ESVLKVFVDL YNKGLIYRGV RMVNWDPKAL
TALSDEEVIY KEEHGKLFYL RYKIEGEDGY AVVATTRPET IMGDTAMCIN PNDPKNQHLK
GKKVIVPLVG RVIPVIEDDY VDIEFGTGCL KVTPAHDVND YMLGEKYNLP SIDIFNDNGT
ISEAAGMYIG MDRFDVRKQI EKDLEAAGLL EKTEAYTNKV GYSERTNVVI EPKLSMQWFL
KMEHLAQIAL EPVMKDDIKF YPAKYKNTYR HWMENIKDWC ISRQLWWGHR IPAYFLPEGG
YVVAVTDEEA LKLAREKTGN PNLKMTDLRQ DEDCLDTWFS SWLWPISLFD GINNPGNEEI
NYYYPTSDLV TGPDIIFFWV ARMIMAGYEY EGKMPFKNVY FTGIVRDKLG RKMSKSLGNS
PDPLELIEKY GADGVRMGMM LSAPAGNDIL FDDALCEQGR NFCNKIWNAF RLVKGWENGM
GTIDIPADAH LAVQWFDQRL DAAAVEVADL FSKYRLSEAL MLIYKLFWDE FSSWLLEIVK
PAYGQPVNGF IYSMTLSAFE RLLAMLHPFM PFITEELWQQ LREREPGASL MVQPLGEPGE
VNEEFLQQFE TAKEIISSVR TIRLQKNIAL KEPLELQVVG ANPVEKMNPV IRKMCNLSAI
EVVDAKADGA SSFMIGTTEF AVPLGNMIDV DAEIARMEAE LKHKEGFLQG VLKKLSNEKF
VNNAPAAVIE MERKKQADAE SIIQSLKESI ASLKNV
