SYV_ACIAD
ID SYV_ACIAD Reviewed; 971 AA.
AC Q6F8F0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ACIAD2950;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(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; CR543861; CAG69665.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F8F0; -.
DR SMR; Q6F8F0; -.
DR STRING; 62977.ACIAD2950; -.
DR PRIDE; Q6F8F0; -.
DR EnsemblBacteria; CAG69665; CAG69665; ACIAD2950.
DR KEGG; aci:ACIAD2950; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000430; 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; Reference proteome.
FT CHAIN 1..971
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224426"
FT COILED 906..933
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 971 AA; 110101 MW; 6851172240BA1B50 CRC64;
MIFIMTDAHA QSAQNIATTY DPTDIERKWY QIWEEKGYFK PSGQGDSFCI MIPPPNVTGS
LHMGHGFNNA IMDALTRYNR MMGKNTLWQP GTDHAGIATQ MVVERQLAAQ NISRHDLGRE
QFIDKVWEWK EQSGGTITKQ IRRLGSSVDW SRERFTMDDG LSNAVKEVFV KLHEDGLIYR
GKRLVNWDPK LQTALSDLEV ESVEEKGSLW HFKYFFEDKS LKTQDGHDFL VVATTRPETL
LGDTAVAVHP EDERYAHLIG KNIVLPITGR LVPIVADEYV EKDFGTGCVK ITPAHDFNDY
DLGKRHDLPI INIFNKNAEV LAEFEYIAKA GEQISDAIAA PADYVGLERF AARKKLVAQA
EAEGWLDQIQ PYDLKAPRGD RSGVIVEPLL TDQWYVKIAP LAQPAIEAVQ DGRIKFVPEQ
YTNMYMAWMN NIQDWCISRQ LWWGHRIPAW YDAEGNVYVG RNEEEVRAKN NLAADLALQQ
DEDVLDTWFS SGLWTFSTLG WTGDAKKDAE NYFLNTFHPT DVLVTGFDII FFWVARMIMM
TMHFMKNEDG TPQVPFKTVY VHGLVRDGEG QKMSKSKGNV LDPLDLIDGI DLESLVQKRT
FGLMNPKQAE KIEKATRKEF PEGINSYGTD AVRFTFCALA NTGRDIKFDL KRVEGYRNFC
NKIWNATRFV LMNVEGQTVA QEARPELWEL PEQWIMSRLQ KAEQAVHQAF ATYRLDLAAQ
TIYDFIWNEY CDWYVELTKP VLNDAEVSEE RKAEVRRVLL AVMEASLRLA HPLMPYLTEE
IWQTLAPMIG KGGDTIMTAK YPVPEAAKMN EQAEADMQWL QGLIGAVRNI RGEMGLGNAR
LLPVLLQNIS DSERTQIERI QPLFKALAKV ESITFLAQGE EPPLSSSSVV GHASVFVPMK
GLIDPKAELG RLQKDLDKVQ KQHDQIASKL ANEGFVAKAP AAVVEGEKVK LAEFADQLVK
IKQSMEQIAA L
