ID A0A4Q4ZMY1_9ACTN Unreviewed; 868 AA.
AC A0A4Q4ZMY1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
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 ECO:0000313|EMBL:RYP88981.1};
GN ORFNames=EKO23_00660 {ECO:0000313|EMBL:RYP88981.1};
OS Nocardioides guangzhouensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2497878 {ECO:0000313|EMBL:RYP88981.1, ECO:0000313|Proteomes:UP000295198};
RN [1] {ECO:0000313|EMBL:RYP88981.1, ECO:0000313|Proteomes:UP000295198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130 {ECO:0000313|EMBL:RYP88981.1,
RC ECO:0000313|Proteomes:UP000295198};
RA Fu Y., Cai Y., Lin Z., Chen P.;
RT "Nocardioides guangzhouensis sp. nov., an actinobacterium isolated from
RT soil.";
RL Submitted (JAN-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_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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYP88981.1}.
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DR EMBL; SDKM01000001; RYP88981.1; -; Genomic_DNA.
DR RefSeq; WP_134713031.1; NZ_SDKM01000001.1.
DR AlphaFoldDB; A0A4Q4ZMY1; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000295198; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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:UP000295198}.
FT DOMAIN 34..625
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 63..73
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 868 AA; 96819 MW; 5E7B2DE30A0C5130 CRC64;
MTETPTRTDL SETTPQRAVV VPDKPALEGL ESRWVETWKS DDTYRFDRSQ TRENVYSIDT
PPPTVSGSLH VGHVFSYTHT DLIARYQRMT GKSVFYPMGW DDNGLPTERR VQNYYGVRCD
PSLPYDEGFT PPEKPDPKRQ VPISRPNFVE LCEELVQADE EVFEQLWRTL GLSVDWKEHY
TTIGPKAQAV SQRAFLRNFA RGEAYLQEAP TLWDVTFQTA VAQAELEARD YAGHYHRVAF
HRADGSPVHI ETTRPELIPA VVALIAHPDD ERYADLFGQT VTSPVFGVQI PVLPHPLAEP
DKGAGIAMCC TFGDLTDVQW WRELNLPVRT VIGRDGRLHR ETPEWLAAAD AAYQQLAGKT
AFSAREAMVA LLRESGDLEG DPTPTQRMTN FYEKGDKPLE IVATRQWYIR NGGRNAELRA
EMLEHGAEIT WSPAHMKHRY DNWVAGLNGD WLISRQRFFG IPFPVWYPLD EEGEPDYDHP
LLPTEAELPL DPTTVAPRGY DEAQRGKPGG FLADPDVMDT WATSSLTPHI AGGWTTDDDL
WQRVFPMDLC TQAHDIIRTW LFSRVVRAHY ENGVAPWSHA MVSGFILDPD RKKMSKSKGN
VVVPTDVLEK YGADAVRWRA AMARPGLDSP FDETQMKVGR RLAMKVLNAS KFVLGSVGAT
APTPSAISDP VDCALMGRLA NTVTAATEAF DAYDYTTALE VAERFFWEFC DDYLELVKER
AYAEDGGIAT ASAKATLALA LHVQLRLLAP FLPYVTEEVW SWWQEGSVHR AAWPKATDLG
SSAASNDSIM TAVAAALTGI RGAKSQAKVS MRAELSRVEL TGTAAMIDGI RKAEQDLRQA
CKISGDLVLT EDEGAEELRV DATLAETA
//
