ID A0A1H4NYI4_9MICC Unreviewed; 871 AA.
AC A0A1H4NYI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 36.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005};
GN ORFNames=SAMN04489745_1817 {ECO:0000313|EMBL:SEC00270.1};
OS Arthrobacter woluwensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=156980 {ECO:0000313|EMBL:SEC00270.1, ECO:0000313|Proteomes:UP000182652};
RN [1] {ECO:0000313|EMBL:SEC00270.1, ECO:0000313|Proteomes:UP000182652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10495 {ECO:0000313|EMBL:SEC00270.1,
RC ECO:0000313|Proteomes:UP000182652};
RA de Groot N.N.;
RL Submitted (OCT-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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; FNSN01000003; SEC00270.1; -; Genomic_DNA.
DR RefSeq; WP_066210520.1; NZ_FNSN01000003.1.
DR AlphaFoldDB; A0A1H4NYI4; -.
DR STRING; 156980.SAMN04489745_1817; -.
DR Proteomes; UP000182652; Unassembled WGS sequence.
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 Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR NCBIfam; NF000540; alt_ValS; 1.
DR NCBIfam; NF009687; PRK13208.1; 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 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; 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_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Reference proteome {ECO:0000313|Proteomes:UP000182652}.
FT DOMAIN 29..628
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 675..816
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 592..596
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 871 AA; 96681 MW; 3F7E9B16942A5431 CRC64;
MTDATQGTDT PEATTVPDKP ALEGLEAKLT ERWLAEGTYK FQQDTTRGEV YSIDTPPPTA
SGSLHVGHMF SFTQTDVLAR YQRMQGKNVF YPMGWDDNGL PTERRVQNYY GVRCDPAIPY
QEGYQPPAEP AKNQRDWDVV SRRNFIELCE RLAVEDEKIF EHLFKTLGLS VDWDMTYRTI
DDASRAVSQR AFLENHAAGD AYLAEAPTLW DVTFRTAVAQ AELEDREVAG AYHRYPFFTE
DGEKIFIETT RPELLAACAA LVANPDDERY QPLFGKKVTS PLFGVEVEVK AHPLAKADKG
SGIAMVCTFG DLTDVTWWRE LQLPTRAIIG RDGRVLAETP EWITTDAGRE AYERIAGKTA
FSAKEAVVEM LREQDLLDGE PKKIMHAVNF FEKGDKPLEV VTSRQWYIRN GGRDEDRRER
LIQRGREIDF HPAFMRSRYE NWIEGLNGDW LVSRQRFFGV PVPVWYALDS EGNPDYESPI
VPTDDMLPVD PAADAAPGYS EDQRGVPGGF IGDADVLDTW ATSALTPQIV GGWSRDEELF
AKVFPFDLRP QGHDIIRTWL FSSVVRADAL QDVAPWKHAA ISGWILDPDR KKMSKSKGNV
VVPTAVLEEF GSDAVRYWAS SAKLGADTAY EIAQMKIGRR LAIKLLNASK FVLNLGATEA
SVLTADSAVL TNALDRGLLT QLAEVVRQAT DAFEKYDYAR ALQVTESFFW QFTDDYLELI
KDRAYGAQGE EGQASVLAAL ATTLDALLRL FAPFLPFATE EVWSWWRTGS VHRAAWPAPL
EGIDGDVTLL ATVGEALSGL RKAKSEAKVK QRTEVLQATV SGPAARIAQL EAGLADLKAA
ANAREVSLVA ADGELTVSDV ELAPAEAPAQ A
//
