Sequences associated with phospholipid transport were obtained from the Uniprot database and compared to the coat proteins of the Chinese wheat mosaic virus using the built-in MEME program. There are PhoLip ATPase N and PhoLip ATPase C domains in the coat protein of the Chinese wheat mosaic virus, as shown in Table . PhoLip ATPase C and PhoLip ATPase N share similar structures. The coat protein has active sites for the phospholipid transporter flipse at positions 234-520. PhoLip ATPase may still rely on Mg2+-ATP for its conformational change in energy because a Mg2+-ATP binding site, A243, is located here. Cysteine is present in PhoLip ATPase N and PhoLip ATPase C. By flipping the lipids in viral and cellular membranes, the PhoLip ATPase domain makes the membrane less stable. 3.9 The manner that the Chinese wheat mosaic virus invaded plant cells