The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 24: Endonuclease III homolog

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 3 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity GO:0000703
Catalysis of the removal oxidized pyrimidine bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar. The reaction involves formation of a covalent enzyme-pyrimidine base intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apyrimidinic (AP) site.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0003906
Catalysis of the cleavage of the C-O-P bond in the AP site created when DNA glycosylase removes a damaged base, involved in the DNA base excision repair pathway (BER).
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
Oxidized purine nucleobase lesion DNA N-glycosylase activity GO:0008534
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)

There are 5 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
DNA repair GO:0006281
The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
Base-excision repair GO:0006284
In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
Base-excision repair, AP site formation GO:0006285
The formation of an AP site, a deoxyribose sugar with a missing base, by DNA glycosylase which recognizes an altered base in DNA and catalyzes its hydrolytic removal. This sugar phosphate is the substrate recognized by the AP endonuclease, which cuts the DNA phosphodiester backbone at the 5' side of the altered site to leave a gap which is subsequently repaired.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
Cellular response to oxidative stress GO:0034599
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
6 P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP)
Positive regulation of mitochondrial DNA replication GO:0090297
Any process that increases the rate, frequency or extent of the process in which new strands of DNA are synthesized in the mitochondrion.
6 P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP) P31378 (/IMP)

There are 3 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
6 P31378 (/HDA) P31378 (/HDA) P31378 (/HDA) P31378 (/HDA) P31378 (/HDA) P31378 (/HDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
6 P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA) P31378 (/IDA)
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