ProRule PRU00763
General rule information
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Accession | PRU00763 |
Dates | 2-MAR-2009 (Created)
13-FEB-2023 (Last updated, Version 12) |
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 (END4_GEOTN); Q966U0 (END4_DICDI); Q5UPY4 (END4_MIMIV); Q10002 (APN1_CAEEL); |
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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