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DTDA_KORCO
ID   DTDA_KORCO              Reviewed;         276 AA.
AC   B1L7I3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00562};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00562};
DE   AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN   Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; OrderedLocusNames=Kcr_0050;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
CC   -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate specificity.
CC       By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules,
CC       this enzyme counteracts the toxicity associated with the formation of
CC       D-aminoacyl-tRNA entities in vivo. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC         H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC         Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00562};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- SIMILARITY: Belongs to the DtdA deacylase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00562}.
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DR   EMBL; CP000968; ACB06810.1; -; Genomic_DNA.
DR   RefSeq; WP_012308707.1; NC_010482.1.
DR   AlphaFoldDB; B1L7I3; -.
DR   SMR; B1L7I3; -.
DR   STRING; 374847.Kcr_0050; -.
DR   EnsemblBacteria; ACB06810; ACB06810; Kcr_0050.
DR   GeneID; 6093339; -.
DR   KEGG; kcr:Kcr_0050; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_056464_1_0_2; -.
DR   InParanoid; B1L7I3; -.
DR   OMA; CYEATHH; -.
DR   OrthoDB; 84039at2157; -.
DR   PhylomeDB; B1L7I3; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00562; Deacylase_DtdA; 1.
DR   InterPro; IPR018033; Deacylase_DtdA_archaea.
DR   InterPro; IPR007508; DtdA.
DR   PANTHER; PTHR34667; PTHR34667; 1.
DR   Pfam; PF04414; tRNA_deacylase; 1.
DR   PIRSF; PIRSF016210; UCP016210; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..276
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345213"
SQ   SEQUENCE   276 AA;  30777 MW;  F731085A3DB89CE6 CRC64;
     MSKRLALAYS KKDPAGSGMA REIKDMMGEE FEISDKRCEL IEVDREILYI NGSQFEGFDY
     LAVLSRHSGT PNHPIFTAHV SGNFGRARYG GDHFKLSIAI PSLMKEYLIS VSKRAEEIGY
     WVGFEPTHHG PTLDIPTAFL EIGCDETAWR DERGLRAAAE SVLEAIESWK DGKFVAAVAF
     GGPHINDHFT RVELFTRFAI GHAARKLDAE WVDGEMVKQA VSRNGEPTGV AIVDNKGLKG
     EDRERIEGAL RDLGLEVIRV KKILRDELGE EEGEEI
 
 
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