Skip to main content
. 2022 Apr 21;23(9):4588. doi: 10.3390/ijms23094588

Figure 1.

Figure 1

Comparative analysis of protein domains for caspase and metacaspase in human, yeast, and plant. (A). Protein domains for human caspase-1, caspase-2, and caspase-3 are marked using a simple modular architecture research tool (SMART) [14]. Caspases are classified into inflammatory and apoptotic according to their functions, and apoptotic caspases are further divided into initiators and effectors. Initiator caspases have a pro-domain containing a CARD, or death effector domain (DED), at the N-terminus, and effector caspases have a very short pro-domain. Human caspases have conserved active sites (His and Cys) in the large subunit p20. (B). Yeast contains one metacaspase in its genome and has a pro-domain in the N-terminus. There is no special linker between subunits p20 and p10, and active sites (His and Cys) are conserved in subunit p20. (C). Arabidopsis thaliana contains three type I and six type II metacaspases, and type I has an N-terminal pro-domain with or without a zinc-finger at the N-terminus. Type II lacks a pro-domain, but it is characterized by a long linker between subunits p20 and p10. The active sites (His and Cys) are conserved in subunit p20.