ID A0A974SV99_9RHOO Unreviewed; 946 AA.
AC A0A974SV99;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN ORFNames=GBK02_06760 {ECO:0000313|EMBL:QRM19113.1};
OS Dechloromonas sp. TW-R-39-2.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Rhodocyclales; Azonexaceae; Dechloromonas.
OX NCBI_TaxID=2654218 {ECO:0000313|EMBL:QRM19113.1, ECO:0000313|Proteomes:UP000663379};
RN [1] {ECO:0000313|EMBL:QRM19113.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TW-R-39-2 {ECO:0000313|EMBL:QRM19113.1};
RA Choi A.;
RT "Complete Genome Sequence of Dechloromonas sp. TW-R-39-2.";
RL Submitted (OCT-2019) 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:0000256|HAMAP-Rule:MF_02004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:0000256|ARBA:ARBA00047552, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|ARBA:ARBA00060830,
CC ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP045202; QRM19113.1; -; Genomic_DNA.
DR RefSeq; WP_203468973.1; NZ_CP045202.1.
DR KEGG; dech:GBK02_06760; -.
DR Proteomes; UP000663379; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 CDD; cd00817; ValRS_core; 1.
DR FunFam; 3.40.50.620:FF:000457; Predicted protein; 1.
DR FunFam; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000009; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.90.740.10:FF:000005; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; NF004349; PRK05729.1; 1.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000663379}.
FT DOMAIN 16..620
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 676..823
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 881..946
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 879..906
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 543..547
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 946 AA; 107282 MW; F02A0E7171F41D9E CRC64;
MELAKAFEPA DIERRWYPEW ESQNYFAAGV DRSKAPDENF CILLPPPNVT GTLHMGHGFN
QTIMDALTRY YRMRGHNTLW QPGTDHAGIA TQIVVERQLD AQGISRHDLG REKFLEKVWE
WKEYSGNTIT KQMRRMGTSP DWKRERFTMD AGLNTVVNET FVRLFNEGLI YRGKRLVNWD
PKLNTAVSDL EVVQEEEDGF MWHIRYPLAD GSDSLVVATT RPETMLGDTA VMVHPEDERY
KHMIGKLVKL PLTGREIPII ADSYVDLEFG TGCVKVTPAH DFNDYAVGQR HGLPMISILT
LDAKINESAP EKYRGLDRFD ARKAVVADLE AEGILIKVDK HKLKVPRGDR TNVVIEPMLT
DQWFVAMSKP GEDGKSITEK ALDVVHSGEI KFYPENWVNT YNQWLNNIQD WCISRQLWWG
HQIPAWYGDN GEIFVARNEE EARAEASKQG YTGSLKRDDD VLDTWFSSAL WPFSTLDWTG
DEAIDAANPI LQQYLPSTVL VTGFDIIFFW VARMVMMTKQ ITGQIPFKHV YVHGLIRDGE
GQKMSKSKGN VLDPIDLIDG IDLEKLIEKR TTGLMNPKQA ESIAKKTKKE FPEGIASFGT
DALRFTFASL ASPGRDIKFD LNRCDGYRNF CNKLWNATRF VLMNVEGHDL ALDHKQGGDG
ACTVDGEKRL KFSFADRWIV SQLQRVEQEV ERHFTDYRFD LIAQAIYKFV WDEFCDWYLE
IAKVEIQTGD EAQQRGARRT LIRTLEAVLR LAHPLIPFIT EELWQTVAPI AGRKTHDSIM
LADYPRADLT RLDPASEAKV ERLKALAYAC RNLRGEMNVS PALRMPLLVA GGGDEMADFA
PILQALGKLS EVQLVDDMPT DAVAPVAVVG ETRLMLKVEI DVAAEKVRLA KEIEKLEKQI
SIAQNKLGNE GFVARAPAAV IDQEKQRVAD FTATLEKLKP QLAKLG
//
