ID I2MY78_STRT9 Unreviewed; 873 AA.
AC I2MY78;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=STSU_024435 {ECO:0000313|EMBL:QKM69824.1};
OS Streptomyces tsukubensis (strain DSM 42081 / NBRC 108919 / NRRL 18488 /
OS 9993).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1114943 {ECO:0000313|EMBL:QKM69824.1, ECO:0000313|Proteomes:UP000005940};
RN [1] {ECO:0000313|EMBL:QKM69824.1, ECO:0000313|Proteomes:UP000005940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993
RC {ECO:0000313|Proteomes:UP000005940};
RX PubMed=22740677; DOI=10.1128/JB.00692-12;
RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M.,
RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F.,
RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z.,
RA Rodriguez-Garcia A., Tauch A., Martin J.F.;
RT "Draft genome of Streptomyces tsukubaensis NRRL 18488, the producer of the
RT clinically important immunosuppressant tacrolimus (FK506).";
RL J. Bacteriol. 194:3756-3757(2012).
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; CP029159; QKM69824.1; -; Genomic_DNA.
DR RefSeq; WP_006349311.1; NZ_CP029159.1.
DR AlphaFoldDB; I2MY78; -.
DR Proteomes; UP000005940; 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}.
FT DOMAIN 28..567
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 612..754
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..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 811..866
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 530..534
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 873 AA; 97316 MW; 76DFB26D206BF97E CRC64;
MTENTQQQPA STPELPTQYA PAEVEGTLYE RWVGRGYFEA DAKSEKTPYT VVIPPPNVTG
SLHMGHAFEH TLIDALTRRK RMQGYETLWQ PGMDHAGIAT QNVVERELAK EGKSRHDLGR
EAFVDRVWQW KAESGGQIQG QMRRLGEGVA WSRDRFTMDE GLSRAVRSVF KKMYDDGLIY
RAERIINWCP RCLTAISDIE VDYQDDDGEL VSLKYGEGDE TLVVATTRAE TMLGDTAVAV
HPDDERYAHL IGKRIKLPLT DRSIPVVADT HVDPEFGTGA VKVTPAHDPN DFAIGQRHGL
ESIEVLDERG IITVHGPFQG LDRFEARSAI VAALRAEGRI VAEKRPYTHS VGHCSRCRTT
LEPRVSLQWW VKVEPLAKAA GDAVREGKVA IHPADMTQRY YDWVDNMHDW CISRQLWWGH
RIPVWHGPNG EMVAVGPDEE PPAGEGWEQD PDVLDTWFSS GLWPFSTLGW PEQTPDLEKF
YSTDVLVTGY DLMFFWVARM MMFGLYAMDG EPPFRTVAFH GMVRDEFGKK MSKSAGNTVN
PLDWMDTYGS DAVRFTLARG ANPGTDVPIG EDWVQASRNF ANKIWNATRF ALMNGATVEG
ELPAAEELSA ADRWILSRLN KTVADVDAFY DDYQFAKLSD ALYHFAWDEV FDWYVELSKT
TYFAGGDQAK VSARVLGEVL DVSLRLLHPV MPFVTEALWT TLTGRESVVV ADWPADSGFR
DEAAEREIEL VQRVVTEVRR FRSDQGLQPG QKVPARLDLA GTSLAPHEAA IRQLLRLQPE
GDSFSATATL PVAGASVALD LSGTIDVAAE RKRLAKDLAV AEKEKAQAEA KLGNEAFLAK
APDQVVDKIR GRLASAEADI ARITNQLAAL PTA
//
