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annotation rule: PRU00763

General rule information [?]

Accession PRU00763
Dates 2-MAR-2009 (Created)
21-NOV-2019 (Last updated, Version 8)
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.

Propagated annotation [?]


Description [?]

case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa>
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>
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase 1; EC 4.2.99.18; AltName: Full=Apurinic-apyrimidinic endonuclease 1; Short=AP endonuclease 1;
else case <OC:Viruses>
AltName: Full=Putative endonuclease 4; EC 3.1.21.2; AltName: Full=Endonuclease IV;
end case


Comments [?]

case <OC:Bacteria> or <OC:Archaea>
Function Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin.
Catalytic activity Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.; EC=3.1.21.2;
else case <OC:Fungi> or <OC:Nematoda>
Function DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA.
Catalytic activity Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.; EC=4.2.99.18;
else case <OC:Amoebozoa> or <OC:Viruses>
Function Plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues.
Catalytic activity Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.; EC=3.1.21.2;
end case

case <OC:Eukaryota>
Subcellular location Nucleus.
end case

Cofactor Zn(2+)
Note: Binds 3 Zn(2+) ions.
Similarity Belongs to the AP endonuclease 2 family.

Cross-references [?]

case <Feature:PS51432:67=H>
PROSITE PS00729; AP_NUCLEASE_F2_1; 1;
end case

case <Feature:PS51432:177=D> and <Feature:PS51432:180=H>
PROSITE PS00730; AP_NUCLEASE_F2_2; 1;
end case

case <Feature:PS51432:214=H> and <Feature:PS51432:227=D> and <Feature:PS51432:229=H>
PROSITE PS00731; AP_NUCLEASE_F2_3; 1;
end case


Gene Ontology [?]

GO:0006974; Biological process: cellular response to DNA damage stimulus.
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 <OC: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 <OC:Fungi> or <OC:Nematoda>
GO:0003906; Molecular function: DNA-(apurinic or apyrimidinic site) endonuclease activity.
GO:0016829; Molecular function: lyase activity.
end case

case <OC:Eukaryota>
GO:0005634; Cellular component: nucleus.
else case <OC:Bacteria> or <OC:Archaea>
GO:0005737; Cellular component: cytoplasm.
end case


Keywords [?]

case <OC:Bacteria> or <OC:Archaea> or <OC:Amoebozoa> or <OC:Viruses>
else case <OC:Fungi> or <OC:Nematoda>
end case

case <OC:Eukaryota>
end case


Features [?]

From: PS51432
Key     From     To       Description   Tag   Condition   FTGroup
METAL     67     67       Zinc 1     H  
METAL     107     107       Zinc 1     H  
METAL     143     143       Zinc 1     E  
METAL     143     143       Zinc 2     E  
METAL     177     177       Zinc 2     D  
METAL     180     180       Zinc 3     H  
METAL     214     214       Zinc 2     H  
METAL     227     227       Zinc 3     D  
METAL     229     229       Zinc 3     H  
METAL     259     259       Zinc 2     E  

Additional information [?]

Size range 240-305 amino acids
Related rules None
Repeats 1
Topology Undefined
Examples A4IR02 (END4_GEOTN); Q966U0 (END4_DICDI); Q5UPY4 (END4_MIMIV); Q10002 (APN1_CAEEL): [Recover all]
Scope
Bacteria
Archaea
Eukaryota
Viruses
Comments None

Copyright

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 [?]