SYV_DEIRA
ID SYV_DEIRA Reviewed; 913 AA.
AC Q9RY06;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=DR_0148;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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:0000255|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:0000255|HAMAP-Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; AE000513; AAF09735.1; -; Genomic_DNA.
DR PIR; E75554; E75554.
DR RefSeq; NP_293872.1; NC_001263.1.
DR RefSeq; WP_010886794.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RY06; -.
DR SMR; Q9RY06; -.
DR STRING; 243230.DR_0148; -.
DR EnsemblBacteria; AAF09735; AAF09735; DR_0148.
DR KEGG; dra:DR_0148; -.
DR PATRIC; fig|243230.17.peg.313; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR InParanoid; Q9RY06; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR11946; PTHR11946; 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; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..913
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106223"
FT COILED 851..912
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 544..548
FT /note="'KMSKS' region"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 913 AA; 102748 MW; 58865899DFC2A227 CRC64;
MTDPHTTTLP TQFDPTGIEP KWAARWRSEP FRADATSGKD PFTIVIPPPN VTGNLHLGHA
LDNTLIDTLI RYKRMAGFEA LYLPGMDHAG ISTQVVVERQ LKDAGTSRHD LGREAFLEKV
WEWKGKSGGM ILDQLTRLGV SADWTRERFT MDEGLSRAVR TQFVKLYHDG LAYRGERIVN
WDPASQTTLS ELEIDREVRK GKMYTLSYKL ENSAERGSNG ETGEIRIATV RPETIFADQA
IAVHPEDERF RHLVGQKARI PLTDRWVPII ADEAVEMEFG VGALKITPAH DPTDFEVGER
HGLERPSVID LDGNLTRDEL VPAEFQGLER FAARKAVVKA LEESGDLLEQ KDHDTAIGLS
ERTKVPVEPI ISEQWFVKMK PFADQVLEGL DKGEIKLVPE RYTKVNRDWL ENIRDWNISR
QLWWGHQIPA WYDKEGNIYV PDPENPELDC DQDPRYAHLN LRRDPDVFDT WFSSNLWPFS
TLGWPDTDSE DFRKFYPTQV LVTGYDILFF WVARMQMAGY GLTGQAPFST VMLHGLYLDA
KGQKMSKSKG NGIDPLELFG QYGVDACRFA FTFLSTGGQD IKHDARRFEQ GRNFANKLWN
ATRFALMRLG EARIEGSDDL SAYVRAAVTL PDGVLLRSKD VLAQLKERDD LTLADRWIIS
RLNDVTAEAS AQLDAFDIGA AIRTLYSFTW DEFCDWYIEA AKPELASGNL GTMATLKVVL
EHVLKLLHPF MPFITSELYA ALGHRRQIAV HSWPQPDAAL HDAEATKAFD ALRSAVDSAR
SLKSELGLSP QDRLNVAVDG DLADVVRQNA RVVEGIARVN LVPALEGRTL SQVAPGVTIL
APLEGTVDIA DWVKKQQKRL AELDKQIKQA QGKLNNEGFV ARAPAEVIEE EKRRVADFGA
QKERLEGVLA QLG