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Rpn9 C-terminal helix The 26S proteasome is the major ATP-dependent protease in eukaryotes which plays a key role in intracellular protein degradation. The lid of the 26S proteasome contains six PCI-domain-containing proteins (Rpn3/5/6/7/9/12), two MPN-domain-containing proteins (Rpn8/11), and one peptide, Sem1. The only catalytically active member of the lid is Rpn11, which serves as the essential deubiquitinase of the proteasome. The C terminus of each subunit in the lid is predicted to form one or more helices. These C-terminal helices are highly conserved and have been predicted to form a helical bundle structure. In yeast, Rpn9 was found to be necessary for the integrity and efficiency of the 26S proteasome. This entry represents a helix domain C-terminal to the PCI domain found in Rpn9, a subunit of the 26S proteasome. C-terminal truncations of Rpn5 or Rpn9 have been shown not to cause any major lid assembly defects but to prevent the association of Rpn12. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",