SYV_BDEBA
ID SYV_BDEBA Reviewed; 894 AA.
AC Q6MQK8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Bd0458;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX842647; CAE78439.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6MQK8; -.
DR SMR; Q6MQK8; -.
DR STRING; 264462.Bd0458; -.
DR PRIDE; Q6MQK8; -.
DR EnsemblBacteria; CAE78439; CAE78439; Bd0458.
DR KEGG; bba:Bd0458; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000008080; 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_0000224442"
FT COILED 827..852
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 894 AA; 102267 MW; 8D9C8BF6AF3191AF CRC64;
MKMSEQLSDR YNPADVESRT YEWWEKNGYF KAQDQSTKPP FSIILPPPNV TGFLHMGHAL
DHTIQDMMIR WKRMNGYNTM WLPGTDHAGI ATQSVVEREL KKDGVTRHDL GREKFVEKVW
DWKHQYGNRI YGQMRRLGDS CDWDRAVFTL DEGVSKAVRK VFVSLHKKGL IYRGQRLVNW
SGPLETAISD LEVEHKQIKG SLYHVKYPLE DGSGFLVVAT TRPETMLGDS AVCVHPEDER
YKHLIGKNVL LPLTNRKIKI IADTYVDKEF GSGVVKITPA HDFNDYKIGK THNLEFINIL
TKKAEINENG GVYAGLKVQE ARKRILEDLK AQDLLEKEEP HVHSVGHCSR SGAVVEPYLS
EQWFVKMEAL AVPAKRVAEN GTIRFEPESW TKVYLHWLNN IEDWCISRQL WWGHRIPVWY
CEDCNHQTVA ETDVTACEKC GSTKLHQDDD VLDTWFSSAL WPFSTMGWPN ETETLKTFYP
TSYLVTGHDI IFFWVARMIM MGLEFQRDVP FRTVYIHGLV RDSQGRKMSK SLGNSIDPVE
MIEKHGADAL RFTFAAHLYS GKDFKFSEQR LEGYRNFMNK VWNAARFALS NLSDFKAPTE
GVKALPNKVH ISVFDQWIIT KLEEVTKTVE EAMEQERFSD ASTALYQFIW NQFCDWYIEF
TKPILNGNNA EEKAATQLVI AQVLNRIMRL LHPFAPFISE EIYQKLPIKG TACIVDQYPN
ARNDKEFLSL GSAQAALEID IVKEVITAIR NIRGENRISP AVKLNVRLGV TNDQTQKILG
NNRTALMTMG RLENMEIGPE GDMMKCAVAP VVVKDASVKV IIPLEGLVDF DEEVKRINKS
IEKLTRDIGM LSGKLSNEKF VANADEEVVA ADRALLAQSK VQLDSLRDAL TRFQ
