The domain within your query sequence starts at position 17 and ends at position 212; the E-value for the ATG16 domain shown below is 1.8e-13.
WKRHIVRQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWR EEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRL EALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLL EQLVQRKARAAAERNL
ATG16 |
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PFAM accession number: | PF08614 |
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Interpro abstract (IPR013923): | 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. It is found in the vacuole [ (PUBMED:11689437) ]. 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. Auotphagy protein 16 (Atg16) has been shown to be bind to Atg5 and is required for the function of the Atg12p-Atg5p conjugate [ (PUBMED:10406794) ]. Autophagy protein 5 (Atg5) is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway [ (PUBMED:10712513) ]. This entry represents autophagy protein 16 (Apg16), which is required for the function of the Apg12p-Apg5p conjugate. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATG16