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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.
Amos Bairoch

ProRule PRU00764


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00764
General rule information [?]

Accession PRU00764
Dates 02-MAR-2009 (Created)
13-FEB-2023 (Last updated, Version 13)
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; P44318;

Propagated annotation [?]

Identifier, protein and gene names [?]

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 [?]

case <OC:Eukaryota>
SUBCELLULAR LOCATIONNucleus.
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 LOCATIONCytoplasm.
end case
SIMILARITYBelongs to the DNA repair enzymes AP/exoA family.

Keywords [?]

DNA damage
DNA repair
Hydrolase
Metal-binding
Nuclease
case <OC:Eukaryota>
Endonuclease
Nucleus
else case <OC:Bacteria>
Cytoplasm
Exonuclease
Magnesium
end case

Gene Ontology [?]

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 [?]

PROSITE PS00726; AP_NUCLEASE_F1_1; 1;
PROSITE PS00727; AP_NUCLEASE_F1_2; 1;
PROSITE PS00728; AP_NUCLEASE_F1_3; 1;

Features [?]

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 [?]

Size range 230-370 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

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 [?]