SYV_DECAR
ID SYV_DECAR Reviewed; 943 AA.
AC Q47BG6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Daro_3085;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ47815.1; -; Genomic_DNA.
DR RefSeq; WP_011288813.1; NC_007298.1.
DR AlphaFoldDB; Q47BG6; -.
DR SMR; Q47BG6; -.
DR STRING; 159087.Daro_3085; -.
DR EnsemblBacteria; AAZ47815; AAZ47815; Daro_3085.
DR KEGG; dar:Daro_3085; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
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.
FT CHAIN 1..943
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224470"
FT COILED 875..934
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 541..545
FT /note="'KMSKS' region"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 943 AA; 106500 MW; 9CB7A2DAC73D3442 CRC64;
MELAKAFEPA DIERRWYPEW ETQNYFAAGV DASKADNFCI LLPPPNVTGT LHMGHGFNQT
IMDALTRYYR MRGHNTLWQP GTDHAGIATQ IVVERQLDAQ GISRHDLGRE KFLEKVWEWK
EYSGNTITKQ MRRMGTSPDW KRERFTMDAG LNKVVTETFV RLFNEGLIYR GKRLVNWDPK
LNTAVSDLEV VQEEEDGFMW HIRYPLADGS DSLVVATTRP ETMLGDTAVM VHPEDERYKH
MIGQMVKLPL TDREIPIIAD SYVDLEFGTG CVKVTPAHDF NDYAVGQRHG LPMISILTLD
AKVNENAPEK YRGLDRFDAR KAVVADLEAL GILEKTDKHK LKVPRGDRTN VVIEPMLTDQ
WFVAMSKPGD DGKSITEKAL DVVHSGEIKF YPENWVNTYN QWLNNIQDWC ISRQLWWGHQ
IPAWYGDNGQ IFVAHSEAEA KAEAAKQGYT GTLKRDEDVL DTWFSSALWP FSTLDWTGDE
AIDAANPLLK QYLPSSVLVT GFDIIFFWVA RMVMMTKQIT GQIPFKHVYV HGLIRDGEGQ
KMSKSKGNVL DPIDLIDGIG LEALIEKRTT GLMNPKQAES IAKKTKKEFP EGIASFGTDA
LRFTFASLAS PGRDIKFDLN RCDGYRNFCN KLWNATRFVL MNVEGHDLAL EHQQNGPACG
GSAPLEFSFA DRWIVSQLQR VEQEVEQHFT DYRFDLIAQA IYKFIWDEFC DWYLEIAKVE
IQTGNDAQQR GARRTLVRTL EAVLRLAHPL IPFITEELWQ TVAPIAGRKT HDSIMLAAYP
RAEEYKIDAA SEAKVERLKA LAYACRNLRG EMNVSPALRM PLLVAGGGAE ISEFAAILQA
LGKLSEVQIV DDMPADAMAP VAVVGETRLM LKVEIDVAAE RIRLAKEIEK LEKQISIAQG
KLANEGFVAR APAAVIDQEK QRVADFTATL EQLKPQLAKL GQA
