ProRule PRU00764
General rule information
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| PURL | https://purl.expasy.org/prosite/rule/PRU00764 |
| Accession | PRU00764 |
| Dates | 2-MAR-2009 (Created)
13-FEB-2023 (Last updated, Version 12) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51435; AP_NUCLEASE_F1_4 |
Name | AP endonucleases family 1 |
| Function | Exonuclease III and AP endonuclease 1 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) |
Eukaryota Bacteria |
| Example(s) | P28352 (APEX1_MOUSE); P44318 (EX3_HAEIN); |
Propagated annotation
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Identifier, protein and gene names
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| case <OC:Eukaryota> | |
| Protein name | AltName: Full=DNA-(apurinic or apyrimidinic site) endonuclease; EC=3.1.-.-; |
| else case <OC:Bacteria> | |
| Protein name | AltName: Full=Exodeoxyribonuclease III; Short=Exonuclease III; Short=EXO III; EC=3.1.11.2; |
| end case | |
Comments
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| case <OC:Eukaryota> | |
| SUBCELLULAR LOCATION | Nucleus. |
| else case <OC:Bacteria> | |
| CATALYTIC ACTIVITY | Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; |
| SUBCELLULAR LOCATION | Cytoplasm. |
| end case | |
| SIMILARITY | Belongs to the DNA repair enzymes AP/exoA family. |
Keywords
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| DNA damage | |
| DNA repair | |
| Hydrolase | |
| Metal-binding | |
| Nuclease | |
| case <OC:Eukaryota> | |
| Endonuclease | |
| Nucleus | |
| else case <OC:Bacteria> | |
| Cytoplasm | |
| Exonuclease | |
| Magnesium | |
| end case | |
Gene Ontology
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| GO:0003677; Molecular function:DNA binding | |
| GO:0004519; Molecular function:endonuclease activity | |
| GO:0006281; Biological process:DNA repair | |
| case <OCellular component:Eukaryota> | |
| GO:0003906; Molecular function:DNA-(apurinic or apyrimidinic site) endonuclease activity | |
| GO:0005634; Cellular component:nucleus | |
| else case <OCellular component:Bacteria> | |
| GO:0000287; Molecular function:magnesium ion binding | |
| GO:0008311; Molecular function:double-stranded DNA 3'-5' DNA exonuclease activity | |
| GO:0005737; Cellular component:cytoplasm | |
| end case | |
Cross-references
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| PROSITE | PS00726; AP_NUCLEASE_F1_1; 1; |
| PROSITE | PS00727; AP_NUCLEASE_F1_2; 1; |
| PROSITE | PS00728; AP_NUCLEASE_F1_3; 1; |
Features
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| From: PS51435 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 258 | 258 | /note="Proton acceptor" | H | ||||||||
| BINDING | 7 | 7 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
N | ||||||||
| BINDING | 40 | 40 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
E | ||||||||
| BINDING | 158 | 158 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
| BINDING | 160 | 160 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
N | ||||||||
| BINDING | 257 | 257 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
| BINDING | 258 | 258 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
H | ||||||||
Additional information
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| Size range | 230-370 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
Archaea [1] Bacteria [7] Eukaryota [22] All [ 30 ]
- Retrieve set of proteins with 3D structure for this domain