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The UL27 open reading frame of the Duck Plague virus encodes glycoprotein B, the molecular characteristic of this gene was analyzed with bioinformatics software. The results indicated that this gene encodes an estimated 1000 putative proteins, contains the conserved domain of the Herpesvirus UL27-like protein. Similarity comparisons of DPV CHv strain gB protein sequences with those of 20 known herpesviruses clearly showed that the DPV gB protein sharing 58.0%, 48.1%, 45.9%, 45.8%, 45.8%, 45.8% and 39.4% amino acid identity with MDV, PRV, EFV-1, HSV-1, EHV-4, BHV-2 and ILTV, respectively. Phylogenetic tree of the amino acids sequences showed this gene has a close evolutionary relationship with MDV, indicating that the DPV should be placed into a single cluster within the subfamily Alphaherpesvirinae. The relative molecular weight of the protein was 113.8781kDa, an obvious transmembrane region was located between 860aa-883aa with a signal peptide 1aa-20aa. Nine N-glycosylation sites, fifteen N-myristoylation sites, four cAMP- and cGMP-dependent protein kinase phosphorylation sites, twenty Protein kinase C phosphorylation sites, seventeen Casein kinaseIIphosphorylation sites, three Tyrosine kinase phosphorylation sites and one Amidation site were determined by PROSCAN. Also, one Cell attachment sequence R-G-D was located in site 525aa-527aa. These results provided rational data to elucidate biological function and physiological features of the UL27 gene.