| Primary Identifier | IPR042527 | Type | Homologous_superfamily |
| Short Name | Atg5_UblA_dom |
| description | Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Atg proteins coordinate the formation of autophagosomes. The pre-autophagosomal structure contains at least five Atg proteins: Atg1p, Atg2p, Atg5p, Aut7p/Atg8p and Atg16p, found in the vacuole [, ]. The C-terminal glycine of Atg12p is conjugated to a lysine residue of Atg5p via an isopeptide bond. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. Autophagy protein 16 (Atg16) has been shown to bind to Atg5 and is required for the function of the Atg12p-Atg5p conjugate []. Autophagy protein 5 (Atg5) is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway [].Atg5 comprises two ubiquitin-like domains that flank a helix-rich domain. The N- and C-terminal ubiquitin-like domains are called UblA and UblB, respectively, and the helix-rich domain between UblA and UblB, is called HR. Both UblA and UblB comprise a five-stranded -sheet and two-helices, which is a conserved feature in all ubiquitin superfamily proteins. The HR domain consists of three alpha helices [].This superfamily represents the UblA domain. |
