Abstract

This report showed some physicochemical properties and structural features about DPV-UL13 protein predicted by some software and online tools. The online analysis of the physicochemical properties demonstrates that the protein has thirty-four potential phosphorylation sites when the threshold of prediction score is above 0.5 and both the signal peptide and the transmembrance region are not found. In addition, the protein has hydrophilic amine acid districts more than hydrophobic districts and subcellular localization largely locates at mitochondrial with 43.5%. The secondary structure results revealed that random coils dominated among secondary structure elements followed by alpha helix and extended strand. The phylogenetic tree shows that DPV-UL13 protein has close evolutionary relationship with the genus Mardivirus. And the multiple sequences alignment of UL13 protein in 156-436 sequence among DPV, HSV-1 and Mardivirus genus suggests highly conserved characteristic. These analysis surpports the guess that DPV-UL13 product may be a Ser/Thr protein kinase. All the data will be a basis for the further functional study of the DPV-UL13 protein.

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