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IPR018085 is a Uracil-DNA glycosylase, active site.
<p>Uracil-DNA glycosylase [ec:3.2.2] (UNG) [[cite:PUB00000054]] is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved [[cite:PUB00001176]] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [[cite:PUB00004816]]. In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human UNG1 protein is transported to both the mitochondria and the nucleus [[cite:PUB00004423]]. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation [[cite:PUB00004423]], but the presence of a mitochondrial transit peptide has not been directly demonstrated. The most N-terminal conserved region contains an aspartic acid residue which has been proposed, based on X-ray structures [[cite:PUB00004202], [cite:PUB00000916]] to act as a general base in the catalytic mechanism.</p> <p>This signature pattern covers the most N-terminal conserved region, which contains an aspartic acid residue that has been proposed, based on X-ray structures [[cite:PUB00004202], [cite:PUB00000916]] to act as a general base in the catalytic mechanism.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | DNA repair | 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. | ||
| Molecular function | Hydrolase activity, hydrolyzing N-glycosyl compounds | Catalysis of the hydrolysis of any N-glycosyl bond. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: uracil-DNA glycosylase-like [Glycine max] gi|356544588|ref|XP_003540731.1| | 16 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd10027 | CDD | 1 | 100.00 |