(data stored in ACNUC30630 zone)

SWISSPROT: 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   11-DEC-2019, entry version 126.
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}.
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   SMR; Q9RY06; -.
DR   STRING; 243230.DR_0148; -.
DR   PRIDE; Q9RY06; -.
DR   EnsemblBacteria; AAF09735; AAF09735; DR_0148.
DR   GeneID; 1799158; -.
DR   KEGG; dra:DR_0148; -.
DR   PATRIC; fig|243230.17.peg.313; -.
DR   eggNOG; ENOG4105CA4; Bacteria.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020093; -.
DR   InParanoid; Q9RY06; -.
DR   KO; K01873; -.
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   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; 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   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;
DR   PRODOM; Q9RY06.
DR   SWISS-2DPAGE; Q9RY06.
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                   /note="ATP"
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
//

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