Turkish Journal of Biology




Aspartic proteases (APs; EC: 3.4.23) are a catalytic type of protease enzymes that use an activated water molecule, bound to one or more aspartate residues, for catalysis of their peptide substrates. In this study, bioinformatic analyses of APs enzymes were performed on insect protein sequences, including nineteen species of eleven different families. According to the conserved motifs obtained with MEME and MAST tools, three motifs were common to all insects. The structural and functional analyses of five selected insects from different orders were performed with ProtParam, SOPMA, SignalP 4.1, TMHMM 2.0, and ProDom tools in the ExPASy database. The tertiary structure of Apis mellifera as a sample of insects was predicted by the Phyre2 server using the "1qdm" model (PDB accession code: 1qdm) and was compared with Swiss-Model. The 3D structure quality was verified by the PROCHECK server. MegAlign was used for protein sequence alignment, and a phylogenetic tree was constructed with MEGA 6.06 software using the neighbor-joining method. In protein-protein interaction analysis with STRING 9.1, zero and twenty-seven significant protein interaction groups were identified in A. mellifera and other species, respectively. The obtained data provide a background for bioinformatic studies of the function and evolution of other insects and organisms.

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