From the UniProt database, we downloaded glycophorin-related proteins. We then used the MEME local version tool to compare them one by one to viral proteins in order to identify conserved domains. Table summarizes the results of combining the motifs by protein and domain. According to Table , the viral proteins had a 4.1m domain. The Band 4.1 protein is a two-subunit globular protein. It acts as a promoter of spectrin-actin binding in the membrane skeleton by binding to spectrin. The 4.1m domain can interact with the red blood cell membrane's 4.1 protein. .1m domains are also found in neurexins, syndecans, and glycophorin C. Syndecan-4 is a heparan sulfate-containing transmembrane proteoglycan. It is a co-receptor for cell adhesion with integrin. As a result, the SARS-CoV-2 protein can also adhere to the red blood cell membrane via the heparin system. As is shown in Table , 4.1m A is in the S1 protein's N-terminal domain and is involved in receptor binding. S 4.1m B-D is on the S2 protein's transmembrane and outer membrane side and is involved in membrane fusion. It demonstrates that the S protein bends the erythrocyte membrane via its heparin-like domain. Through the 4.1m domain, S is anchored to band 4.1. ORF3a created pores in the membrane of the host cell. ORF3a 4.1m A is located outside the transmembrane zone and contains the "CWKCR" heme-binding region. ORF3a is bound to band 4.1 via the 4.1m domain. RdRP is a 4.1m-domain-containing membrane-bound protein RNA polymerase. It shows that the virus will replicate itself using immature red blood cells after infection.