Evolutionary Relationships and Distribution Pattern of Cytochrome P450 Enzymes Among Melampsora Species Using In-Silico Approaches

Cytochrome P450s (CYPs) form one of the most notable protein families that are ubiquitously present in all spheres of life. They regulate fungal pathogenic virulence by neutralizing the antifungal compounds synthesized and released by hosts. This study was conducted to elucidate the diversity and abundance, evolutionary relationships and cellular localization of 224 cytochrome P450 in 7 Melampsora species. Eight phylogenetic groups were identified from the total number of CYPs protein sequences. A total of 14 and 13 CYPs families and clans, respectively, were recognized. Eleven cytochrome P450 families: Cyp63, Cyp5025, Cyp5139, Cyp5093, Cyp5035, Cyp53, Cyp597, Cyp526, Cyp5147, Cyp5152 and Cyp5015 were identified to be abundantly domiciled in Melampsora, hence, implying a vital conserved functional activity by these proteins in the Melampsora genus. The endoplasmic reticulum was established to be the primary location of the CYPs. The non-ribosomal peptide synthetase-like (NRPS-like), a gene cluster associated with secondary metabolic activity, was observed to be dominant across all the seven selected Melampsora species except in M. allii-populina 12AY07 v1.0 2, where polyketide synthase-like (PKS-LIKE) dominated. The proliferation of CYPs families in Melampsora, which is linked to the evolution of several fungal traits, including their pathogenicity, is indicated by the prevalence of several cyp clans and families. Hence, results obtained provided a solid foundation that could be explored using biotechnological tools to effectively manage Melampsora species causing diseases in economic tree crops worldwide. Keywords: Cytochrome P450, in-silico, Melampsora, metabolites, phylogenomics.