Muhummadh Khan, Kaiser Jamil
Phylogenetic reconstruction has attracted much attention from biologists and computer scientists from gene order data in recent years. Ubiquitin is widespread in eukaryotes and plays a central role in selective ATP-dependent protein degradation in cells. It is also highly expressed in several types of cancers. Therefore, in order to understand its diversification in eukaryotes, we undertook this study to determine its phylogeny using various computational methods. All the sequences of the ubiquitin-conjugating enzyme were extracted from the Protein Data Bank (PDB), and using the maximum likelihood method as implemented in PHYML, the unrooted phylogenetic tree was constructed. This tree had four major clusters and one mini cluster. We calculated the divergence of the gene clusters from the site-specific change of functional importance in the protein sequence evolution. The divergence was then mapped onto the 3D structure of the ube2c protein obtained from the PDB database: (IL7K) using RASMOL. From this study, we concluded that we were able to identify the exact sites where active E2 evolution is taking place and that it is evident that these sites are subject to strong purifying selection. We believe that this information could have useful implications in the field of neoplasia, as there are reports that mutations in this protein are likely to promote tumor progression.