Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR002043 is a Uracil-DNA glycosylase family 1.
<p>Uracil-DNA glycosylase [ec:3.2.2] (UDG, 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. UDGs were classified into 4 families [[cite:PUB00080616], [cite:PUB00080617]].</p> <p>Family 1 enzymes are active against uracil in both ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions [[cite:PUB00080617]]. Family 1 enzymes are present in Eubacteria, Eukarya and in some eukaryotic viruses. The sequence of uracil-DNA glycosylases is extremely well conserved [[cite:PUB00001176]] in bacteria and eukaryotes as well as in herpes viruses [[cite:PUB00095219]]. 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 nuclear UNG2 and mitochondrial UNG1are both encoded by the UNG gene [[cite:PUB00004423], [cite:PUB00080625]]. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation [[cite:PUB00004423]]. The catalytic C-terminal domains of UNGs are highly conserved at both the sequence and structure level while the N-terminal domains are diverse and are thought to be involved in subcellular localisation and protein-protein interactions [[cite:PUB00095219]].</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 |
|---|---|---|---|---|
| Molecular function | Uracil DNA N-glycosylase activity | Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine. | ||
| 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. | ||
| Biological process | Base-excision repair | 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. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: uracil-DNA glycosylase-like [Glycine max] gi|356544588|ref|XP_003540731.1| | 11 | ||
| – | 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 | 50.00 |