Figure 3

In-Silico analysis point towards functional integrity of Sfp53, despite having structural dissimilarities with human/B. mori/Drosophila p53. (a) Sequence alignment of Sfp53 with human/B.mori/Drosophila p53 showed no considerable similarities. Also (b) Sfp53 did not possess typical 9 amino acid transactivation domain 1 & 2. (c) Protein sequence of Sfp53 was used for the ab-initio modelling using I-TASSER online tool and the protein model (Left panel) was verified by engendering Ramchandran plot (right panel). (d) N-terminus of modelled Sfp53 (blue solid dots model) showed possible interaction with lepidopteran TAF9 (purple solid dots model). Ribbon model on the right panel showed the interaction site (red solid dots) which corresponds to the amino acids 17–25 of Sfp53. (e) DNA binding domain of Sfp53 was observed to have perfect sequence conservation with human p53 for the amino acids known to interact directly with DNA. Further (f) dimerization potential of Sfp53 was analyzed by docking two individual subunits of the C-terminus of Sfp53. (g) The N and C terminus of p53 from S. frugiperda and human were analyzed for their phosphorylation score. Selectively C-terminus of Sfp53 was predicted to be hyper-phosphorylated. Also (h) Sfp53 was predicted to be in hypo-acetylated state.