ProRule PRU00763
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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 ) |
| 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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