CATH Superfamily 1.10.8.50
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: waiting to be named.
FunFam 7: endonuclease 8-like 1 isoform X1
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 8 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 |
---|---|---|
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).
|
1 | Q96FI4 (/TAS) |
Protein C-terminus binding GO:0008022
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|
1 | Q96FI4 (/IPI) |
Protein C-terminus binding GO:0008022
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
|
1 | Q8K4Q6 (/ISO) |
Hydrolase activity, acting on glycosyl bonds GO:0016798
Catalysis of the hydrolysis of any glycosyl bond.
|
1 | Q96FI4 (/IDA) |
Hydrolase activity, acting on glycosyl bonds GO:0016798
Catalysis of the hydrolysis of any glycosyl bond.
|
1 | Q8K4Q6 (/ISO) |
Lyase activity GO:0016829
Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
|
1 | Q8K4Q6 (/IDA) |
DNA N-glycosylase activity GO:0019104
Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.
|
1 | Q8K4Q6 (/IDA) |
DNA N-glycosylase activity GO:0019104
Catalysis of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site.
|
1 | Q96FI4 (/TAS) |
There are 8 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.
|
1 | Q8K4Q6 (/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.
|
1 | Q96FI4 (/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.
|
1 | Q8K4Q6 (/ISO) |
Response to oxidative stress GO:0006979
Any process that results in a change in state or activity of a cell or an organism (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.
|
1 | Q96FI4 (/IDA) |
Response to oxidative stress GO:0006979
Any process that results in a change in state or activity of a cell or an organism (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.
|
1 | Q8K4Q6 (/ISO) |
Negative regulation of nuclease activity GO:0032074
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
|
1 | Q96FI4 (/IDA) |
Negative regulation of nuclease activity GO:0032074
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
|
1 | Q8K4Q6 (/ISO) |
Depyrimidination GO:0045008
The disruption of the bond between the sugar in the backbone and the C or T base, causing the base to be removed and leaving a depyrimidinated sugar.
|
1 | Q96FI4 (/TAS) |
There are 7 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.
|
2 | Q8K4Q6 (/IDA) Q96FI4 (/IDA) |
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.
|
1 | Q8K4Q6 (/ISO) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | Q96FI4 (/IDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | Q8K4Q6 (/ISO) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | Q96FI4 (/TAS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q96FI4 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8K4Q6 (/ISO) |