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ProRule PRU00392
General rule information
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Accession | PRU00392 |
Dates | 7-FEB-2005 (Created)
11-JAN-2024 (Last updated, Version 17) |
Data class | Domain; |
Predictors |
PROSITE; PS51068; FPG_CAT |
Name | Formamidopyrimidine-DNA glycosylase catalytic domain |
Function | DNA glycosylase |
Scope(s) |
Eukaryota Bacteria Archaea |
Example(s) | P05523 (FPG_ECOLI); |
Propagated annotation
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Identifier, protein and gene names
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Comments
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FUNCTION | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. |
CATALYTIC ACTIVITY | Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'- deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3- dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'- deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA- COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; |
SIMILARITY | Belongs to the FPG family. |
end case |
Keywords
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case <FTGroup:1> | |
DNA damage | |
DNA repair | |
DNA-binding | |
Glycosidase | |
Hydrolase | |
Lyase | |
Multifunctional enzyme | |
end case |
Gene Ontology
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case <FTGroup:1> | |
GO:0006974; Biological process:DNA damage response | |
GO:0006281; Biological process:DNA repair | |
GO:0003677; Molecular function:DNA binding | |
GO:0016798; Molecular function:hydrolase activity, acting on glycosyl bonds | |
GO:0016787; Molecular function:hydrolase activity | |
GO:0016829; Molecular function:lyase activity | |
GO:0003824; Molecular function:catalytic activity | |
end case |
Features
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From: PS51068 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 1 | 1 | /note="Schiff-base intermediate with DNA" | P | 1 | |||||||
ACT_SITE | 2 | 2 | /note="Proton donor" | E | 1 | |||||||
ACT_SITE | 57 | 57 | /note="Proton donor (in beta-elimination)" | K | 1 |
Additional information
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Size range | 70-150 amino acids |
Related rules |
None |
Fusion | None |
Repeats | 1 |
Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Bacteria [507] Eukaryota [10] Viruses [2] All [ 519 ]
- Retrieve set of proteins with 3D structure for this domain