Abstract
This report showed some physico-chemical properties and structural features about UL41 protein predicted by some software and on-line tools. The analysis showed both the signal peptide and the trans membrance region are not found. Meanwhile, the protein has twenty-four potential phosphorylation sites. In addition, the protein has more hydrophilic amine acid districts than hydrophobic districts and subcellular localization mainly located at the cytoplasm with 56.5%. The prediction of secondary structure showed that random coils dominate among secondary structure elements followed by alpha helix and extended strand. The prediction of tertiary structure showed the structure of the UL41 protein had a certain level of similarity to the structure-specific nuclease FEN-1(flap endonuclease-1). The study will be a basis for the further functional study of the UL41 protein.
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