Bioinformatics Analysis of the Protein Structure and Function of Helicoverpa armigera CCE001a

ZHANG Li;WANG Hai-liang;MA Xue-er;College of Animal Science and Technology, Shihezi University;

CCE001a;;Carboxylesterase;;Detoxification;;Protein modification sites;;Biological information

[Objective]In order to further predict the protein structure and biological function of CCE001 a.[Method]This study used a bioinformatics method to predict the protein encoded by this gene, and predict its function and structure. [Result] The prediction results show that the total number of amino acid residues of the protein is 556, its molecular formula is C2865 H 4321 N737 O811 S23, the isoelectric point pI of the protein is 5.32, and the positively charged amino acid residues(Arg+Lys) are 58, which are negatively charged. There are 75 amino acid residues(Asp+Glu), protein instability coefficient is 35.22, fat coefficient is 75.91, total average hydrophilicity coefficient is-0.262; CCE001 a protein has a dehydrogenase superfamily(cl21494) domain; analysis shows that α-helix and irregular coils are the main secondary structures of this protein. They account for 31.35% and 46.49%, respectively, including 3.96% of β-turns and 18.20% of extended stretched chains. After tertiary structural prediction, it is shown that the protein includes α-helix and β-turn; the protein subcellular is confirmed to be located in the endoplasmic reticulum, and there is a signal peptide sequence, which can be initially considered as secretory Hydrophilic protein, and no transmembrane protein, a total of 37 phosphorylation sites, one N-glycosylation site. [Conclusion]This study can provide a theoretical basis for studying the detoxification mechanism of CCE001 a.