1.A.120.1.1
The coronaviral  double membrane-spanning pore complex in the replication organelle (RO) of the viral double membrane vesicle (DMV). The pore consists of a hexameric complex. The primary constituent of each of the six subunits of the pore is the non-structural protein-3, nsp3, of 2309 aas, which may have 5 TMSs, based on a hydrophathy plot of the protein. These are clustered together about two-thrids of the way towards the C-terminus. It is the core constituent of the pore and has both its N-terminal domain of 160 kDa and a smaller C-terminal domain, which contains a ubiquitin domain (Ubi1) of 12.6 kDa, that together form the prongs of the cytoplasmic crown. nsp3 interacts with nsp4, and this complex is believed to drive membrane pairing and participate in DMV biogenesis (Wolff et al. 2020). It may associate with other viral and host proteins.