ID A0A0M8SMV8_9ACTN Unreviewed; 859 AA.
AC A0A0M8SMV8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=ADK54_22165 {ECO:0000313|EMBL:KOU40628.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU40628.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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}.
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:KOU40628.1}.
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DR EMBL; LGDD01000288; KOU40628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8SMV8; -.
DR PATRIC; fig|1415557.3.peg.4912; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
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; 2.
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; 2.
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 13..420
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 432..553
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 598..741
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 792..856
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 790..852
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 516..520
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 859 AA; 96107 MW; 7418F8E62EBAD1BC CRC64;
MPTQYAPAEV EGKLYERWVE RGYFTADAGS DKDPYTIVIP PPNVTGALHL GHAFQVTLMD
ALTRRKRMQG YETLWLPGMD HAGIATQNKV EQQLAEEGKS RQDLGREAFT ERVWQWKGEY
GGRILGQLKR LGAGLDWSRE RFTMDEGLSK AVQTIFKNLY DDELIYRAER IINWCPRCLT
AISDIEVEYQ DDPGELVSLK YGEGDDTLVV ATTRAETMLG DTAIAVHPDD ERYQHLIGRL
IKLPLTDRSI PVVADTHVDP EFGTGCVKVT PAHDPNDFAI GQRHNLDSIT VMDERGIITV
PGPFQGLDRY EARSAIVGAL KEQGRIVAEK RPYMHSVGHC SRCKTTVEPR LSMQWWVKVG
PLAQAAGDAV RDGRVKIHPE DMSKRYFDWV DNMHDWCISR QLWWGHRIPI WYGPEGQVVC
VGPDEEPPSG EGWRQDPDVL DTWFSSGLWP FSTLGWPEKT PDLEKFYSTD VLLTGHDIIF
FWVARMMMFG LYAMDGEVPF KTVALTGLVR DEFGKKMSKS NPNAVDPIDW MDAYGSDAVR
FTLAKGANPG ADVPIGEDWV QASRNFANKI WNATRFALMN GATVEGELPP VEQLSATDRW
ILSRLNKTVA EVDAYYEDYQ FAKLSESLYH FAWDEVFDWY VELSKTTFFA GGEQAKVSGR
VLGEVLDVML RVLHPIVPFV TDTLWTTLTG GESLVVADWP KDSGFRDEAA EREIELVQQV
VTEVRRFRSD QGLQPGQKVP AELTLTGTAL APHEAAIRQL LRLQPAGEGF HATASLPVAG
ATVALDLSGT IDVEAERKRL TKDLAAAEKE KADANKKLGN EAFLAKAPDN VVDKIRGRLA
KAEADIERIT NQIAALPKG
//
