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Annotation rule MF_03183
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General rule information [?]

Accession MF_03183
Dates 6-MAR-2014 (Created)
7-OCT-2016 (Last updated, Version 6)
Name Endonuclease_III_Nth
Scope Eukaryota
Templates P78549 (NTH_HUMAN); P31378 (NTH1_YEAST); Q08214 (NTH2_YEAST); Q09907 (NTH_SCHPO): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
NTH
case <OC:Vertebrata>
Protein name
RecName: Full=Endonuclease III-like protein 1;
EC=3.2.2.-;
EC=4.2.99.18;
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
Short=DNA glycosylase/AP lyase;
else
Protein name
RecName: Full=Endonuclease III homolog;
EC=3.2.2.-;
EC=4.2.99.18;
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
Short=DNA glycosylase/AP lyase;
end case
case <OC:Vertebrata>
Gene name
NTHL1
else case <OC:Caenorhabditis>
Gene name
nth-1
else case <OC:Saccharomycotina>
Gene name
NTG1
else
Gene name
NTH1
end case

Comments [?]

Function Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Catalytic activity 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.
case <FTGroup:1>
Cofactor [4Fe-4S] cluster
Note: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
end case
case <OC:Mammalia>
Subunit Interacts with YBX1.
end case
case not <OC:Viridiplantae>
Subcellular location Nucleus. Mitochondrion.
end case
Similarity Belongs to the Nth/MutY family.

Keywords [?]

case not <OC:Viridiplantae>
end case
case <FTGroup:1>
end case

Gene Ontology [?]

case not <OC:Viridiplantae>
GO:0005739; Cellular component: mitochondrion.
GO:0005634; Cellular component: nucleus.
end case
GO:0000703; Molecular function: oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity.
GO:0003906; Molecular function: DNA-(apurinic or apyrimidinic site) lyase activity.
GO:0003677; Molecular function: DNA binding.
case <FTGroup:1>
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
end case
GO:0006285; Biological process: base-excision repair, AP site formation.

Cross-references [?]

PROSITE PS01155; ENDONUCLEASE_III_2; 1;
PS00764; ENDONUCLEASE_III_1; 1;
Pfam PF00633; HHH; 1; trigger=Yes;
PF00730; HhH-GPD; 1;
PF10576; EndIII_4Fe-2S; 1;
PIRSF PIRSF001435; Nth; 1;

Computed features [?]

case not <OC:Viridiplantae>
General TransitM; -; 0-1; trigger=yes;
end case

Features [?]

From: NTH_HUMAN (P78549)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     220     220       Nucleophile; for N-glycosylase activity     K  
METAL     290     290       Iron-sulfur (4Fe-4S)     C   1
METAL     297     297       Iron-sulfur (4Fe-4S)     C   1
METAL     300     300       Iron-sulfur (4Fe-4S)     C   1
METAL     306     306       Iron-sulfur (4Fe-4S)     C   1
SITE     239     239       Important for catalytic activity     D  

Additional information [?]

Size range 238-835 amino acids
Related rules None
Fusion None