We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00392
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00392
General rule information
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| Accession | PRU00392 |
| Dates | 04-FEB-2005 (Created)
11-JAN-2024 (Last updated, Version 18) |
| 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; |
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 [508] Eukaryota [10] Viruses [2] All [ 520 ]
- Retrieve set of proteins with 3D structure for this domain