ID A0A5B8A7R9_9BACT Unreviewed; 876 AA.
AC A0A5B8A7R9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=FHG12_19865 {ECO:0000313|EMBL:QDA62662.1};
OS Hymenobacter jejuensis.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Hymenobacteraceae; Hymenobacter.
OX NCBI_TaxID=2502781 {ECO:0000313|EMBL:QDA62662.1, ECO:0000313|Proteomes:UP000305398};
RN [1] {ECO:0000313|EMBL:QDA62662.1, ECO:0000313|Proteomes:UP000305398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J68-5 {ECO:0000313|EMBL:QDA62662.1,
RC ECO:0000313|Proteomes:UP000305398};
RA Srinivasan S.;
RL Submitted (JUN-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}.
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; CP040896; QDA62662.1; -; Genomic_DNA.
DR RefSeq; WP_139517934.1; NZ_CP040896.1.
DR AlphaFoldDB; A0A5B8A7R9; -.
DR KEGG; hyj:FHG12_19865; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000305398; 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; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR Gene3D; 2.170.220.10; -; 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:SF109; VALINE--TRNA LIGASE; 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:UP000305398}.
FT DOMAIN 15..572
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 614..756
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 812..876
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 876 AA; 99773 MW; 33861BAE82D30CEF CRC64;
MSIAKTYTPA DVEAKWYQRW QEQGFFKAKP NPRKPAYSVV IPPPNVTGVL HMGHMLNNTI
QDVLVRRARM QGKEACWVPG TDHASIATEA KVVALLKEKG IEKRDLTREQ FLEHAWEWKE
KYGGIILEQL KKLGASCDWD RTRFTMEPEM TEAVLRVFVD LYRKGQIYRG VRMVNWDPQG
RTAISDEEVV AKETTAKMYY LRYEVVGQDG QFITVATSRP ETIMADVAVA VNPNDERYKH
LHGQKVRIPL LGREIPVITD EYVAMDFGTG GLKVTPAHDL NDYELGVKHN LPVIDILNDD
GTLSEKAVLY VGQDRFAARK QIAKDLQQAG LLDKIEDYAS VLQTSERTGA VIEPRLSLQW
FCKMDEMAKK ALEVVETDEI KLHPPKFKNM YRVWMENIRD WCISRQLWWG QRIPAWYLPD
GSFVVALNEG EALKLAKEKA GNEQLTRADL RQDEDVLDTW FSSWLWPISV FDGFKDPDNP
DINYFYPTDD LVTAPEILFF WVARMIMAGL EYRREVPFRN VYLTGIVRDT QGRKMSKQLG
NSPDPLDLIA EYGADGVRTG MLFSSPAGND LLFDIKLVEQ GRNFSNKLWN AFRLTQGWEV
NSELPFASEK AVEWFGAKLQ TTLTELDEHF AKFRMSDALM TVYKLVWDDF CSVYLEMVKP
AYQQPIDAET LKYTTGYLET LLKLLHPFMP FITEEIWHEL AERGPKDYVC VAPWPKAQPV
AGATDILDRM GKVLDIVAGV RNVRNQKNIG PSKALTLAAK TDEPELLTAY ESVIRKLANV
SELSFVEAGP AAAVSFVQGG SEFFIPLEGH IDLDAERARL QKEIEYAQGF RDSVLKKLSN
EKFVQNAKPD VIERERQKQA DAEAKIAALE QSLAAL
//
