ID A0A1B1YQW3_9GAMM Unreviewed; 1002 AA.
AC A0A1B1YQW3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=PG2T_02270 {ECO:0000313|EMBL:ANX03127.1};
OS Immundisolibacter cernigliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Immundisolibacterales;
OC Immundisolibacteraceae; Immundisolibacter.
OX NCBI_TaxID=1810504 {ECO:0000313|EMBL:ANX03127.1, ECO:0000313|Proteomes:UP000092952};
RN [1] {ECO:0000313|Proteomes:UP000092952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR3.2 {ECO:0000313|Proteomes:UP000092952};
RA Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT "Complete genome sequence of Solimmundus cernigliae, representing a novel
RT lineage of polycyclic aromatic hydrocarbon degraders within the
RT Gammaproteobacteria.";
RL Submitted (MAR-2016) 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=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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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}.
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DR EMBL; CP014671; ANX03127.1; -; Genomic_DNA.
DR RefSeq; WP_068802635.1; NZ_CP014671.1.
DR AlphaFoldDB; A0A1B1YQW3; -.
DR STRING; 1810504.PG2T_02270; -.
DR KEGG; gbi:PG2T_02270; -.
DR InParanoid; A0A1B1YQW3; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000092952; 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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 2.
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; 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:UP000092952}.
FT DOMAIN 14..677
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 719..876
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 935..997
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 931..958
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 600..604
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1002 AA; 112252 MW; C3B7B40E63F96C8F CRC64;
MDKNYDPAAI EQRWYDQWER AGHFKPSGTG EDPFCIVIPP PNVTGSLHMG HAFNNTVMDL
LIRHARMQGR DTLWQVGTDH AGIATQMVVE RQLAAAGQSR HDLGREAFLE RVWQWKAESG
GAITRQLRRL GASCDWSRER FTMDAGLSKA VSEVFVRLHE DGLIYRGKRL VNWDPVLRTA
VSDLEVVSEE EPGHLWHIRY PLADGSGYLT VATTRPETLL GDAAVAVHPD DERYRHLIGK
ALQLPLCDRQ IPVIADDYVD PAFGTGCLKI TPAHDFNDYQ VWLRHRDEPV FATLPNGGLI
NVLTEDAQIK ELRADDLKLG PPDEDGLRMH SGAPLEGAWT IELIPQKYRG LDRYAARQQI
VADLGAAGLL EAVKEHRHAV PRGDRSGAVL EPYLTDQWYV DLTRETRQDG KPGPGGLVAI
TRPALEAVRS RNIKLIPDNW EKTYAQWLEN IQDWCISRQI WWGHRIPVWY DLDGKDYAGN
DEADVRARHN LAADLPLSQD EDVLDTWFSS ALWPFSTLGW PDRTLQLKRY YPTDVLVTGF
DIIFFWVARM VMMGLVMRPA DADADADVVV DPDVDVGIDD NVPFRTVYVH GLVRDHEGQK
MSKSKGNVLD PLDIIDGVDL DTLIAKRTAG LMQPQMAKKI EQATRKQFPQ GIPAYGTDAL
RFTFASQATL GRDIKFDLAR CEGYRNFCTK LWNAARFVLM NTEGMPPLPA EPVRYGPAER
WIRRCLAETI TKVDAAIAEY RLDYVASALY EFAWGGYCDW YIELAKPVLQ EPDADPAHTL
GVRRTLVEVL EALLRLAHPL IPFITEEIWQ QVAPRAGKKG DTIMLAAWPL ALDFDQDAEE
TAEAVAQIGL LVEVVRAVRN LRAELNLPPG QPVPVLLSGD GDVRTRLESN EHLLRRLARV
ASVEWVTDAA APQAAMALVG DLTVRLPLEG LVDASAEMDR LGREIVKLEQ AITRAEARLA
NPAFVDKAPQ DVVDTERARL AEFAEQRATL VAQRERMAAL AG
//