**8. Molecular modelling of the metacaspase 4 from** *Glycine max* **(type II metacaspase)**

For the comprehension of the structural organization of a type II metacaspase, the delimitation of the p20 and p10 domains of the metacaspase 4 from *G. max* was performed by our group, as well as the analysis of its catalytic amino acids residues and the motifs conservation with other metacaspases and caspases, through protein alignment. Also, the tridimensional structure of the protein was predicted. Metacaspase and caspase sequences of organisms from different taxa (**Table 1**) were aligned using the software Clustal X [83] (http://www.clustal.org/). The sequences were obtained from the National Center of Biotechnology Information (http://www. ncbi.nlm.nih.gov/) data bank and given a treatment for removal of prodomains and loops, for adjustment to the alignment. In this process, the works of Vercammen et al. [8] and of Uren et al. [32] were used as a guide to the delimitation of the domains and catalytic residues.

The p20 and p10 domains of the *G. max* metacaspase were confronted to the Protein Data Bank (http://www.wwpdb.org/) for the search of templates for molecular prediction employing the software Swiss Model [84] (http://swissmodel.expasy.org/). The visualization, the analysis, the validation and the improving of the protein structures were performed with the assistance of the software NOC [85] (http://noch.sourceforge.net).


**Table 1.** List of proteins utilized on the analysis of sequence alignment.
