ID 3MG_ENCCU Reviewed; 208 AA.
AC Q8SQI1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 01-MAY-2013, entry version 58.
DE RecName: Full=Probable DNA-3-methyladenine glycosylase;
DE EC=3.2.2.21;
DE AltName: Full=3-methyladenine DNA glycosidase;
GN OrderedLocusNames=ECU05_1590;
GN and
GN OrderedLocusNames=ECU11_0140;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M.,
RA Weissenbach J., Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon
RT cuniculi (microsporidia): a reference map for proteins expressed in
RT late sporogonial stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to
CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA
CC polymer formed by alkylation lesions (By similarity).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3-
CC methyladenine, 3-methylguanine, 7-methylguanine and 7-
CC methyladenine.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family.
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DR EMBL; AL590445; CAD26679.1; -; Genomic_DNA.
DR EMBL; AL590450; CAD25924.1; -; Genomic_DNA.
DR RefSeq; NP_586320.1; NM_001042153.1.
DR RefSeq; NP_597502.1; NM_001041368.1.
DR ProteinModelPortal; Q8SQI1; -.
DR STRING; 6035.ECU11_0140; -.
DR GeneID; 859169; -.
DR GeneID; 859971; -.
DR KEGG; ecu:ECU05_1590; -.
DR KEGG; ecu:ECU11_0140; -.
DR eggNOG; COG2094; -.
DR HOGENOM; HOG000224224; -.
DR KO; K03652; -.
DR OMA; RIGVTCT; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:EC.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:EC.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 3.10.300.10; -; 1.
DR InterPro; IPR011034; Formyl_transferase_C-like.
DR InterPro; IPR003180; PurDNA_glycsylse.
DR PANTHER; PTHR10429; PTHR10429; 1.
DR Pfam; PF02245; Pur_DNA_glyco; 1.
DR SUPFAM; SSF50486; FMT_C_like; 1.
DR TIGRFAMs; TIGR00567; 3mg; 1.
PE 1: Evidence at protein level;
KW Complete proteome; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1 208 Probable DNA-3-methyladenine glycosylase.
FT /FTId=PRO_0000100069.
SQ SEQUENCE 208 AA; 23773 MW; A4A22F1DAD5B443F CRC64;
MDMGIPCSQL ARRLLGKMLC RRIEGRTTKG MIVETEAYLG KEDKACHSYG GRRTERNSAM
YMKAGTCYVY RIYGRYECFN ISSVEAGAGV LVRALEPLCG VSEMRERRGG RVKDRDIANG
PSKLCIAMGI TRREIDKEWI AGSEKIWLEE GREVADPEIV AGRRIGIRNC GEWEEKKLRF
YIRDNEFVSC IRRRELGNRK HGSVQQLP
//
