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ProRule PRU00764


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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 [?]