The EF-hand calcium-binding domain (EF-hand, IPR002048) is shared by numerous calcium-binding proteins belonging to the same evolutionary family. Ca2 binding induces conformational changes in the EF hand motif that activate or deactivate target proteins . EF-hand typically occurs in pairs or in greater numbers. The P/Homo domain (IPR002884) belongs to a group of calcium-dependent endoproteases called prohormone-preprotein convertases (PCs). For the removal of secreted proteins and peptide hormones, P-protein (for proteolytic) activity is essential. Smooth muscle-specific calponin/LIMCH1(IPR001997) binds actin, tropomyosin, and calmodulin, and may play a role in contraction regulation or modulation. The activity of actomyosin MgATPase is suppressed as a result of the protein's interaction with actin. Domain of homology for calponin (Calponin homolog,IPR001715), an ancestral form of the ABD likely originated from the duplication of a domain called the calponin homology (CH) domain. Dockerin domain(PS51766) is in many cellulosomne, a large multienzyme complex, to efficiently degrade polysaccharides found in plant cell walls. The Chinese wheat mosaic virus coat protein was compared to bacterial EF-hand related sequences that were downloaded from the Uniprot database and compared independently using the local MEME tools. Table shows that the coat protein of the Chinese wheat mosaic virus has several interesting features, including an EF-hand, Calponin homology, Dockerin, and P/Homo. The results show that Ca 2+ is needed for both the binding of receptors and the fusion of membranes that coat protein makes happen.