Summary: Methylpurine-DNA glycosylase (MPG)
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Methylpurine-DNA glycosylase (MPG) Provide feedback
Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA.
Literature references
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Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T; , Cell 1998;95:249-258.: Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. PUBMED:9790531 EPMC:9790531
External database links
SCOP: | 1bnk |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003180
Methylpurine-DNA glycosylase (MPG, or alkyladenine DNA glycosylase (AAG)) is a base excision-repair protein, catalyzing the first step in base excision repair by cleaving damaged DNA bases within double-stranded DNA to produce an abasic site. MPG bends DNA by intercalating between the base pairs, causing the damaged base to flip out of the double helix and into the enzyme active site for cleavage. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA [PUBMED:18191412, PUBMED:10440863, PUBMED:11554308, PUBMED:9790531, PUBMED:11106395, PUBMED:14567703, PUBMED:14688248, PUBMED:15990363, PUBMED:12077143, PUBMED:14555760, PUBMED:12323378]. Its action is induced by alkylating chemotherapeutics, as well as deaminated and lipid peroxidation-induced purine adducts [PUBMED:17768096]. MPG without an N-terminal extension excises hypoxanthine with one-third of the efficiency of full-length MPG under similar conditions, suggesting that is function may largely be attributable to the N-terminal extension [PUBMED:17716976].
Although AAG represents one of six DNA glycosylase classes, it lacks the helix-hairpin-helix active site motif associated with other base excision repair glycosylases and is structurally distinct from them.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | alkylbase DNA N-glycosylase activity (GO:0003905) |
DNA binding (GO:0003677) | |
Biological process | base-excision repair (GO:0006284) |
Domain organisation
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (358) |
Full (3281) |
Representative proteomes | UniProt (14922) |
NCBI (20974) |
Meta (356) |
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RP15 (390) |
RP35 (1491) |
RP55 (3222) |
RP75 (5626) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (358) |
Full (3281) |
Representative proteomes | UniProt (14922) |
NCBI (20974) |
Meta (356) |
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RP15 (390) |
RP35 (1491) |
RP55 (3222) |
RP75 (5626) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_3352 (release 5.2) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 358 |
Number in full: | 3281 |
Average length of the domain: | 178.20 aa |
Average identity of full alignment: | 37 % |
Average coverage of the sequence by the domain: | 84.16 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 183 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Pur_DNA_glycoStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pur_DNA_glyco domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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