Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster

Abstract

Recent studies have suggested that chimeric genes may account for the formation and evolution of new genes and functional divergence. However, the biological function of the new chimeric gene CG17196 of Drosophila melanogaster remains unknown, therefore, this study aims to analyze the structure and function of CG17196 protein using bioinformatics methods. Based on the amino acid sequence of CG17196 protein from NCBI database, the bioinformatics analyses were performed, including protein physical and chemical properties, transmembrane region, signal peptide, subcellular localization, domain, tertiary structure, and the phylogenetic tree of CG17196 related proteins from different species. The results showed that CG17196 protein was an unstable hydrophobic protein, performing biological function in the endoplasmic reticulum. It contained DHHC-type zinc finger domain and three transmembrane regions, but without signal peptide. The prediction result of gene ontology showed that the chance that the CG17196 protein actually had palmitoyltransferase activity was 70%. CG17196 protein and its related proteins in Schizosaccharomyces pombe, Ashbya gossypii, Dictyostelium discoideum and Arabidopsis thaliana showed high homology. In conclusion, CG17196 protein belongs to DHHC protein family and contains palmitoyltransferase activity, which may participate in the protein palmitoylation in the endoplasmic reticulum of Drosophila melanogaster, providing theoretical references for further systematic research on the function and evolution of new chimera CG17196.