LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | This entry represents various uracil-DNA glycosylases and related DNA glycosylases ( ), such as uracil-DNA glycosylase [ ], thermophilic uracil-DNA glycosylase [], G:T/U mismatch-specific DNA glycosylase (Mug) [], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) []. These proteins have a 3-layerα/β/α structure.Uracil-DNA glycosylases are DNA repair enzymes that excise uracil residues from DNA by cleaving the N-glycosylic bond, initiating the base excision repair pathway. Uracil in DNA can arise either through the deamination of cytosine to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA polymerase to form U:A pairs [ ]. These aberrant uracil residues are genotoxic []. The sequence of uracil-DNA glycosylase is extremely well conserved [] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses []. |
| Short Name | Uracil-DNA_glycosylase-like_sf |
