The domain within your query sequence starts at position 30 and ends at position 116; the E-value for the APG12 domain shown below is 5.7e-11.
PVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNTIPPTSA TMGQLYEDNHEEDYFLYVAYSDESVYG
APG12 |
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PFAM accession number: | PF04110 |
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Interpro abstract (IPR007242): | 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 the C-terminal domain of Atg12, which is covalently bound to Atg5 [ (PUBMED:9852036) ]. |
GO process: | autophagosome assembly (GO:0000045) |
GO component: | cytoplasm (GO:0005737) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry APG12