Summary: 8-oxoguanine DNA glycosylase, N-terminal domain
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This is the Wikipedia entry entitled "Oxoguanine glycosylase". More...
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Oxoguanine glycosylase Edit Wikipedia article
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8-oxoguanine DNA glycosylase, N-terminal domain Provide feedback
The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity ( EC:22.214.171.124) and DNA lyase activity ( EC:126.96.36.199) . The region featured in this family is the N-terminal domain, which is organised into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket .
Bjoras M, Seeberg E, Luna L, Pearl LH, Barrett TE; , J Mol Biol 2002;317:171-177.: Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. PUBMED:11902834 EPMC:11902834
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012904
The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity ( EC ) and DNA lyase activity ( EC ) [ PUBMED:10706276 ]. The region featured in this family is the N-terminal domain, which is organised into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket [ PUBMED:11902834 ].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||damaged DNA binding (GO:0003684)|
|oxidized purine nucleobase lesion DNA N-glycosylase activity (GO:0008534)|
|Biological process||nucleotide-excision repair (GO:0006289)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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TBP is a transcription factor whose DNA binding fold is composed of a curved antiparallel beta-sheet . This fold is also found in the N terminal region of DNA repair glycosylases. The N terminal domain of DNA glycosylase has only a single copy of the fold, whereas TBP contains a duplication of this fold [2-3].
The clan contains the following 10 members:AdoMet_dc AlkA_N DUF3378 DUF5611 OGG_N Phage_CRI Rep_trans Rol_Rep_N SpmSyn_N TBP
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_29151 (release 14.0)|
|Number in seed:||54|
|Number in full:||2588|
|Average length of the domain:||118.60 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||29.72 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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Unmapped species names
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The tree shows the occurrence of this domain across different species. More...
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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 OGG_N domain has been found. There are 53 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.