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 PRU00763
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00763
General rule information
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| Accession | PRU00763 |
| Dates | 02-MAR-2009 (Created)
13-FEB-2023 (Last updated, Version 13) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51432; AP_NUCLEASE_F2_4 |
Name | AP endonucleases family 2 |
| Function | Endonuclease 4 related enzymes play a role in DNA repair. These nucleases cleave phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. |
| Scope(s) |
Bacteria Archaea Eukaryota Viruses |
| Example(s) | A4IR02; Q966U0; Q5UPY4; Q10002; |
Propagated annotation
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Identifier, protein and gene names
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| case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> | |
| Protein name | AltName: Full=Probable endonuclease 4; EC=3.1.21.2; AltName: Full=Endonuclease IV; AltName: Full=Endodeoxyribonuclease IV; |
| else case <OC:Fungi> or <OC:Nematoda> or <OC:Viruses> | |
Comments
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| case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> | |
| CATALYTIC ACTIVITY | Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end- products.; EC=3.1.21.2; |
| end case | |
Keywords
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| DNA damage | |
| DNA repair | |
| Hydrolase | |
| Endonuclease | |
| Nuclease | |
| case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> | |
| Metal-binding | |
| Zinc | |
| end case | |
| case <OC:Eukaryota> | |
| Nucleus | |
| end case | |
Gene Ontology
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| GO:0006974; Biological process:DNA damage response | |
| GO:0006281; Biological process:DNA repair | |
| GO:0046872; Molecular function:metal ion binding | |
| GO:0008270; Molecular function:zinc ion binding | |
| GO:0003677; Molecular function:DNA binding | |
| case <OCellular component:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> or <OC:Viruses> | |
| GO:0008833; Molecular function:deoxyribonuclease IV (phage-T4-induced) activity | |
| GO:0004519; Molecular function:endonuclease activity | |
| GO:0004518; Molecular function:nuclease activity | |
| GO:0016787; Molecular function:hydrolase activity | |
| else case <OCellular component:Fungi> or <OC:Nematoda> | |
| GO:0003906; Molecular function:DNA-(apurinic or apyrimidinic site) endonuclease activity | |
| end case | |
| case <OCellular component:Eukaryota> | |
| GO:0005634; Cellular component:nucleus | |
| else case <OCellular component:Bacteria> or <OC:Archaea> | |
| GO:0005737; Cellular component:cytoplasm | |
| end case | |
Cross-references
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| PROSITE | PS00729; AP_NUCLEASE_F2_1; 1; |
| PROSITE | PS00730; AP_NUCLEASE_F2_2; 1; |
| PROSITE | PS00731; AP_NUCLEASE_F2_3; 1; |
Features
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| From: PS51432 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 67 | 67 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
H | 1 | |||||||
| BINDING | 107 | 107 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
H | 1 | |||||||
| BINDING | 143 | 143 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
E | 1 | |||||||
| BINDING | 143 | 143 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
E | 2 | |||||||
| BINDING | 177 | 177 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
D | 2 | |||||||
| BINDING | 180 | 180 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
H | 3 | |||||||
| BINDING | 214 | 214 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
H | 2 | |||||||
| BINDING | 227 | 227 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
D | 3 | |||||||
| BINDING | 229 | 229 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3" |
H | 3 | |||||||
| BINDING | 259 | 259 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
E | 2 | |||||||
Additional information
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| Size range | 240-305 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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