Reovirus fold/BTV fold
All capsid proteins have a common fold consisting of three to four domains: -The N-term column runs from top to bottom and connects the other domains. It essentially consists of beta strands; -The helix-rich domain consists mainly of alpha-helixes, which form the five-fold pore of the capsid. In many ghabrivirales it contains a loop having the cap-snatching catalytic activity. -The middle domain varies in different order. In many ghabrivirales it supports the cap-snatching catalytic activity. - The C-term domain consists mainly of beta-strands, except in mindivirales, which are mainly alpha-helixes. It is flexible and forms the three-fold axes and the two-fold axes of the icosahedral capsid.
Origin:
Viral
Topology
Cellular homologs of the double jelly-roll major capsid proteins clarify the origins of an ancient virus kingdom
Mart Krupovic a, Kira S Makarova b, Eugene V Koonin b
Proc Natl Acad Sci U S A. 2022 Jan 25;119(5):e2120620119.
The logic of virus evolution
Eugene V Koonin, Valerian V Dolja, Mart Krupovic
Cell Host Microbe. 2022 Jul 13;30(7):917-929.