ID A0A5C1AJE6_9BACT Unreviewed; 999 AA.
AC A0A5C1AJE6;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 23.
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=PX52LOC_05140 {ECO:0000313|EMBL:QEL18126.1};
OS Limnoglobus roseus.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Gemmatales;
OC Gemmataceae; Limnoglobus.
OX NCBI_TaxID=2598579 {ECO:0000313|EMBL:QEL18126.1, ECO:0000313|Proteomes:UP000324974};
RN [1] {ECO:0000313|Proteomes:UP000324974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX52 {ECO:0000313|Proteomes:UP000324974};
RA Kulichevskaya I.S., Naumoff D.G., Miroshnikov K., Ivanova A.,
RA Philippov D.A., Hakobyan A., Rijpstra I.C., Sinninghe Damste J.S.,
RA Liesack W., Dedysh S.N.;
RT "Limnoglobus roseus gen. nov., sp. nov., a novel freshwater planctomycete
RT with a giant genome from the family Gemmataceae.";
RL Submitted (AUG-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|HAMAP-Rule:MF_02004}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP042425; QEL18126.1; -; Genomic_DNA.
DR RefSeq; WP_149112659.1; NZ_CP042425.1.
DR AlphaFoldDB; A0A5C1AJE6; -.
DR KEGG; lrs:PX52LOC_05140; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000324974; 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:000032; Valine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal 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}; Coiled coil {ECO:0000256|HAMAP-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:UP000324974}.
FT DOMAIN 17..618
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 722..867
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 932..987
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 937..999
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 999 AA; 111565 MW; 7B42C7BAE9CB1EBA CRC64;
MATELPKAYE PKAAQGKWLK FWAAKEYFHA DPAKSGEPYT IVIPPPNVTG ALHMGHALNN
TLQDVLIRWR RMQGRNTLWM PGTDHAGIAT QAVVERLIFN TEKKTRHDLG REALVAKIWE
WKDKYEKRIL GQLQEMGASC DWQRTRFTLD ETCAKAVRET FFRMFRDGYI YRGKRLVNWD
AQLQTSVADD ETYTEDTKGG FWTFKYAVVG QPDTFIRFST TRPETMLGDT ALCVHPSDER
YKALVGKMVL QPLVNREIPI IADALLADPT LGTGCVKVTP AHDPNDYACW TRNPQIGIIN
ILNPDGTINA NGGPYSGQPR AKVREAVVQA MEELGLFEGK EDRVIPLKYS DRSKTPIEPY
LSDQWFVKMT DRDDGKPGLA QTAMDAVTDG RVQFFPKRYE NSYLDWLGEK RDWCVSRQLW
WGHRIPVWRL GPVQMNEDES NGIEGQLDQI ANASPERICW RIETTEPDEG NISTVTFLVC
TGADAASLEA ELAKLGFAQD PDVLDTWFSS ALWPHSTLGW PEATPDLKRY YPTSTLVTSR
DIITLWVARM VMTGLYNTGE VPFRHVVIHP KIMDGFGEGM SKSKGNGVDP LDIIDLYGAD
AMRFGVVSLA TETQDSRMPV SNVCPHCGTL IPQKREHQSG KTRQIVCPGD KAAGVVCGKP
FRPSGPWLEE DPELPTAKGA SERFETGRNF ANKLWNATRF ILMNLEGYSA APLDPNALPT
EDRWILSRLA TTAKAVTEAL EGYRFSEVAR LVYDFAWNEF CDWYIEMSKG RRTDPVCQRV
LVGVLDGIVR LIHPVMPFLA ESLWHALNEA APIRGLLKAE PAGESVAVAP WPGDLDSLID
DTTEGSIARM QELVRGVREI RNRYMLDKAP LDLSVKCSDA TVADLNALAP FIKLLGGITN
FTCGPTAAKP KQAGSILHAQ FEGYVNLAGL IDVPAELKRL EKQIADKKKM LDSIQGKLNN
AGFLAKAAPE QVQETRDKAA ELESQIRTMA ANEAELKAV
//
