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Glycoprotein K encoded by the DEV-UL53 gene is one of the DEV envelope glycoproteins. Like most members of the alphaherpesvirinae, the genes in the UL region of its genome are well conserved, which means that the major DEV envelope glycoprotein K possessing similar functions of envelope glycoprotein K of alphaherpesvirinae plays an essential role in viral replication and cell fusion. Glycoprotein K sequence analysis indicates that the protein possesses typical characteristics of membrane glycoproteins containing five transmembrane helix structures and an NH2-terminal signal peptide cleavage site, which provide some information for its expression. The precursor gK has five hydrophobic domains, which consists of 343 amino acids and exhibits a molecular mass of 38.12 kDa. Through combining the result of estimating potential antigenic epitopes and secondary structure presumption, five B cell dominant epitopes can be initially definited, which locate at 60-62, 144-155, 157-160, 210-214 and 293-294 amino acids. In conclusion, all the data and consequences will provide a basis for further functional study of the DEV-glycoprotein K and provide necessary data for the new type clinical diagnosis of DEV and the development of new DEV vaccine.