4.4 Sequence scanning of Rv2615c protein
Predictions of I-TASSER strongly suggested the similarity of Rv2615c with APAF1-apoptosome structure involved in Caspase activation and cell death pathways followed by in-vitro experiments which further confirmed the apoptogenic role played by Rv2615c protein. It is reported that the APAF1-apoptosome activates the Caspase9 via CARD-CARD interaction between APAF1-Caspase9. Therefore, multiple sequence alignment of Rv2615c was performed with CARD-APAF1 and CARD-Caspase9. The alignment was checked for various conserved and similar residues. Secondary structure of predicted CARD-like domain in Rv2615c was analysed with MINNOU server (Cao et al. , 2006). Structural superimposition of predicted CARD-like domain in Rv2615c with CARD-APAF1 and CARD-Caspase9 was carried out in Pymol software.