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Atg11 middle domain This domain represents the region comprised between residues 522 and 583 from fission yeast protein Atg11, which is necessary and sufficient for Atg11 autophagy function and for supporting Atg1 kinase activity as it harbours an Atg1-binding domain at the N-terminal and a homodimerization domain at the C-terminal. The N-terminal part contains the conserved aromatic residues Phe and Tyr necessary for the direct and specific interaction with the tMIT domain of Atg1. This interaction is required for the autophagy function of Atg11. The C-terminal part of this domain, residues 546-583, is predicted to adopt a coiled-coil conformation which mediates Atg11 homodimerization. It seems to be conserved among Schizosaccharomyces. |
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PubMed References
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Jiyao W et al.(2023). "The conserved domain database in 2023.",