ID A0A1Y0C284_9MYCO Unreviewed; 883 AA.
AC A0A1Y0C284;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 18-JUN-2025, entry version 37.
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=BTO20_11925 {ECO:0000313|EMBL:ART69196.1};
OS Mycobacterium dioxanotrophicus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=482462 {ECO:0000313|EMBL:ART69196.1, ECO:0000313|Proteomes:UP000195331};
RN [1] {ECO:0000313|EMBL:ART69196.1, ECO:0000313|Proteomes:UP000195331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH-06 {ECO:0000313|EMBL:ART69196.1,
RC ECO:0000313|Proteomes:UP000195331};
RA He Y.;
RT "Whole Genome Sequence of 1,4-Dioxane Degrading Bacterium Mycobacterium
RT dioxanotrophicus PH-06.";
RL Submitted (APR-2017) 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|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|ARBA:ARBA00060830,
CC ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP020809; ART69196.1; -; Genomic_DNA.
DR RefSeq; WP_198344353.1; NZ_CP020809.1.
DR AlphaFoldDB; A0A1Y0C284; -.
DR KEGG; mdx:BTO20_11925; -.
DR Proteomes; UP000195331; 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; 1.10.730.10:FF:000027; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000098; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000129; Valine--tRNA ligase; 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 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; 2.
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:UP000195331}.
FT DOMAIN 25..436
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 445..578
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 621..761
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 818..883
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 540..544
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 883 AA; 98090 MW; C8685C598EDDA4D3 CRC64;
MTSTPDNRAD ALPKSWEPGA VEAELYQGWV DAGYFTADAT SDKPAYSIVL PPPNVTGSLH
MGHALDHTLM DVLTRRKRMQ GYEVLWLPGM DHAGIATQTL VEKQLAADGK TKEDFGREEF
VEKVWDWKRE SGGTIGAQMR RIGDGVDWSR DRFTMDDGLS RAVRTIFKRL FDAGLIYQAE
RLVNWSPVLE TAISDLEVKY EDVEGELVSF RYGSMSDDEP HIVVATTRVE TMLGDTAIAV
HPDDERYRHL VGTTLPHPFT DARIIIVADT HVDPEFGTGA VKVTPAHDPN DFEIGLRHQL
PMPTIMDTKG RIADTGTQFD GMDRFEARVK VREALAEQGR IVAEKRPYLH SVGHSERSGE
PIEPRLSLQW WVKVESLAKA AGDAVRGGDT VIHPPSLEPR WFAWVDDMHD WCISRQLWWG
HRIPIWHGPN GETVCVGPDE TPPEGWEQDP DVLDTWFSSA LWPFSTMGWP DHTADLAKFY
PTSVLVTGYD ILFFWVARMM MFGTFVGDDP AITLEGKRGR QVPFQNVFLH GLIRDEFGRK
MSKSRGNGID PLEWVEMFGA DALRFTLARG ASPGGDLSIG EDHARASRNF ATKLFNATRF
ALMNGAAPAA LPPAAELTDA DRWILGRLEE VRAEVDEALD SYQFSRACEA LYHFAWDEFC
DWYVELAKVQ IFGGLPHTTA VLAAVLDTLL KLLHPVMPFV TETLWKTLTG GESAVIAAWP
QPSGFAPDPV AAQRITDMQK LITEVRRFRS DQGLADRQKV PARLSDIAAA QLSEQLPAIT
SLAWLTEAGD GFTPSAAVEV RLSQTTVVVE VDTSGTVDVA AERRRLEKDL AVAQKEMATT
AAKLGNDAFL AKAPAEVVDK IRGRQQVATE EVERITARLA GLK
//
