ID A0A1V0AHR7_9ACTN Unreviewed; 863 AA.
AC A0A1V0AHR7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BKM31_57235 {ECO:0000313|EMBL:AQZ69757.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ69757.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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; CP017717; AQZ69757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0AHR7; -.
DR STRING; 1909395.BKM31_57235; -.
DR KEGG; noa:BKM31_57235; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000190797; 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; 3.
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; 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:UP000190797}.
FT DOMAIN 29..564
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 605..744
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 797..861
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 795..857
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 863 AA; 95743 MW; 3BCC6265A33F2B86 CRC64;
MPASLELGAV TTPELPTQYT PADVETRSYE RWVSEGYFRA DPGSSREPYS IVLPPPNVTG
VLHIGHALDH SIQDALTRRA RMLGRETLWL PGMDHAGIAT QNVVERELAK QGKSRHDLGR
EAFVERVWEW KEESGGRILG QMRKLGDGVD WSRERFTMDP GLSRAVQTIF KKLFDDGLIY
RAERIINWCP RCLTALSDIE VEHSEDEGEL VSIRYSDEIV VATTRAETML GDTAVAVHPS
DERYAHLVGT MVEVPLTGRM IPVVADEHVD PAFGTGAVKV TPAHDPNDFE IGRRHSLPSL
TVMDERGVIT AHGPFEGLDR FEARPAVVAA LRAEGRIVAE KRPYVHSVGH CSRCKTVVEP
RLSLQWFVNV APLAKAAGDA VRDGRTRIHP PELAKRYFDW VDDMHDWCIS RQLWWGHRIP
VWYGPGGEVV CVGPDEEPPA GYTQDSDVLD TWFSSGLWPF STLGWPDRTD ELERFYPTSV
LVTGYDILFF WVARMMMFGL YAMDGEPPFR VVALHGMVRD QYGKKMSKSF GNVVDPLDWV
DRFGADATRF TLLRGANPGA DVAVSEEWAA GSRNFCNKIW NATRFALMNG AAVGSLDGAE
LTAADRWILS RLQSVIEAAD AAFEEFEFAK ASDLLYHFAW DEVCDWYLEL AKIQLGEGLE
HTRLVLGHVL DALLRLLHPL VPFVTEELWR AVTGGESVVV APWPVRDERY ADPAAEAEIE
ALQELVTEVR RFRSDQGLKP GQKVAARLGL SGTPLAGQET AIRSLLRLTD PSESFNATAR
LSVGAVTVEI DTAGAIDVAA ERKRLEKDLA AARKEAAQVA AKLGNEQFMA KAPQDVVAKV
RGRAEQASAD IERLEAQLAA LGV
//
