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MIG_PYRAE
ID   MIG_PYRAE               Reviewed;         230 AA.
AC   Q7LX22; Q9P9L6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Thymine/uracil-DNA glycosylase {ECO:0000305};
DE            EC=3.2.2.- {ECO:0000269|PubMed:10671447};
DE            EC=3.2.2.29 {ECO:0000269|PubMed:10671447};
DE   AltName: Full=Pa-MIG {ECO:0000303|PubMed:10671447};
GN   OrderedLocusNames=PAE3199 {ECO:0000312|EMBL:AAL64746.1};
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   COFACTOR.
RX   PubMed=10671447; DOI=10.1128/jb.182.5.1272-1279.2000;
RA   Yang H., Fitz-Gibbon S., Marcotte E.M., Tai J.H., Hyman E.C., Miller J.H.;
RT   "Characterization of a thermostable DNA glycosylase specific for U/G and
RT   T/G mismatches from the hyperthermophilic archaeon Pyrobaculum
RT   aerophilum.";
RL   J. Bacteriol. 182:1272-1279(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- FUNCTION: DNA glycosylase that excises thymine from T/G mismatches and
CC       uracil from U/G mismatches. Can also process T/GO and U/GO, but not
CC       A/G, T/C and U/C. Has weak AP lyase activity.
CC       {ECO:0000269|PubMed:10671447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes mismatched double-stranded DNA and polynucleotides,
CC         releasing free thymine.; EC=3.2.2.29;
CC         Evidence={ECO:0000269|PubMed:10671447};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:10671447};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster has a structural role.
CC       {ECO:0000250|UniProtKB:P83847};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR   EMBL; AF222335; AAF37270.1; -; Genomic_DNA.
DR   EMBL; AE009441; AAL64746.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7LX22; -.
DR   SMR; Q7LX22; -.
DR   STRING; 178306.PAE3199; -.
DR   EnsemblBacteria; AAL64746; AAL64746; PAE3199.
DR   KEGG; pai:PAE3199; -.
DR   PATRIC; fig|178306.9.peg.2405; -.
DR   eggNOG; arCOG00462; Archaea.
DR   HOGENOM; CLU_012862_2_1_2; -.
DR   InParanoid; Q7LX22; -.
DR   OMA; RNMIRVI; -.
DR   BRENDA; 3.2.2.29; 5239.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR044298; MIG/MutY.
DR   PANTHER; PTHR42944; PTHR42944; 1.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..230
FT                   /note="Thymine/uracil-DNA glycosylase"
FT                   /id="PRO_0000449119"
FT   BINDING         204
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         211
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         214
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
SQ   SEQUENCE   230 AA;  26446 MW;  D29488F5A4F6AAC5 CRC64;
     MCSDLIPRGV DYTKFRDAII KWYREFGEKD LPWRKAGDPW AVLVAALLLR KTTVKQVVDI
     YREFLRRYPS PARLADASVE EIKAIIQPLG MEHVRATLLK KLSEELVRRF NGQIPCDRDA
     LKSLPGVGDY AASEVLLTAC GKPEPLLDRN MIRVIERVFG IKSKKRRPHT DRELWNFARS
     LVPRDPELAK EFNFGVLDFA RKVCTAKSPK CSLCPLANNV CVFYQKRERV
 
 
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