Genetic Diversity Analysis and In Silico Investigation of Post-Translational Modifications of Carboxypeptidase A1 (CpA1) in Sordaria fimicola

Abstract

Post-translational modifications (PTMs) regulate different complex mechanisms of cell and affect cell growth, stress, evolution of living organisms and adaptations due to environment. The purpose of the present research is to investigate the genetic diversity and PTMs of protease (Carboxypeptidase A1) n Sordaria fimicola. They perform a variety of functions ranging from housekeeping: e.g., protein maturation, signal peptide cleavage, signal transduction, intracellular protein turnover, immune response, apoptosis, and reproduction. S. fimicola is a microscopic filamentous fungus, has been preferably used in this study because of its easy growing pattern on Potato Dextrose Agar (PDA) and a short life cycle of 7 to 12 days. The genomic DNA of six of the strains S. fimicola was used to amplify the carboxypeptidases A1 gene (CpA1), the product size was 940 bp. The multiple sequence alignment of the nucleotide sequences of six strains of S. fimicola with Neurospora crassa (as a reference strain) was studied. The numbers of polymorphic sites in six strains of S. fimicola with respect to N. crassa were six. Posttranslational modifications were depicted by using bioinformatics tools i.e., YinOYang1.2, NetPhos 3.1 and NetNES 1.1 Server to calculate O-glycosylation, phosphorylation sites, and nuclear export signals respectively. The study has predicted 19 phosphorylation sites on serine residues for protease Carboxypeptidase A1 in S1 strains of S. fimicola while 15 phosphorylation sites on serine in N7 strain and 17 serine phosphorylation modifications were predicted in N. Crassa. The results of this research will be helpful for further in vitro investigations of this industrially important enzyme under study. © 2021 Friends Science Publishers