ID A0A2W2CQ62_9ACTN Unreviewed; 872 AA.
AC A0A2W2CQ62;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:BCJ60743.1};
GN ORFNames=C1I93_26475 {ECO:0000313|EMBL:PZF87316.1}, Jiend_41650
GN {ECO:0000313|EMBL:BCJ60743.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZF87316.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZF87316.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZF87316.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BCJ60743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109090 {ECO:0000313|EMBL:BCJ60743.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Jishengella endophytica NBRC 109090.";
RL Submitted (AUG-2020) 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; AP023358; BCJ60743.1; -; Genomic_DNA.
DR EMBL; POTX01000273; PZF87316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2CQ62; -.
DR KEGG; meno:Jiend_41650; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000248627; Unassembled WGS sequence.
DR Proteomes; UP000682317; 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; 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}; 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}.
FT DOMAIN 28..432
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 443..564
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 609..750
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 806..870
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 872 AA; 97030 MW; F32F1BC74F7B47EF CRC64;
MTERLDARRP DAPTLAGQYQ PGEVEQRRYE RWVADGRFRA SAESDKPAFT IVIPPPNVTG
SLHMGHALDH TVQDALVRRK RMQGFEALWL PGMDHAGIAT QNVVERQLAG QGLSRHDLGR
DKFVERVWQW KAESGGAILG QMRRLGDSVD WDRERFTMDE GLSRAVGTMF KKLYDDGLIY
RANRIINWCP RCLTALSDIE VEHTDDDGEL VSIRYSDDVV VATTRAETML GDTAVAVHPD
DERYRHLIGT EVELPLTGRR IPIVGDAHVD PAFGTGMVKV TPAHDPNDFE IGQRHNLPSL
TVMDERGVIT VPGPFEGLDR FEARPAIVAA LREQGLIVAE KRPYVHAVGH CSRCRTTVEP
RLSLQWFVNT APLAKAAGDA VRDGRVRIEP AELAKRYFAW VDNMHDWCIS RQLWWGHRIP
VWYGPDGEVV CVGPDEQPPT GEGWHQDEDV LDTWFSSGLW PFSTLGWPER TPELAKFYPT
SVLVTGYDIL FFWVARMMMF GLYAMDGVQP FDVIALHGMV RDEHGKKMSK SFGNVVDPLD
WIDRYGADAT RFTLARGANP GGDVPVSEDW CQGSRNFCNK LWNVTRFALL NGAHTEGPLP
DAAELSTVDR WILSRLAQVT VEVDEQFEGY EFAKVCDLLY HFAWDDVCDW YVELSKPVLA
GGGAPADATR RVLGHVLDQL LRLLHPVIPF VTEELWTALT GGETVLTAAW PVADRARVDA
TAETEVATLQ RVVTEIRRFR SDQGLRPTQR VVARLDGLAD AGLAGHEPLI RSLVRLDPAG
DDFQASATLA MPGEVSVALD TRGTIDVAAE RARLTKDRAA AEKEAGQARA KLDNPAFVGK
APEHVVAKIR ERLAVAEADL TRIDAALEAL PS
//
