Identification of protein sectors in the primary structure of SMS and GDI1. A) Distribution of the protein sectors within the different regions of human spermine synthase. The analyzed residues correspond from position 28 to 365 based on the structure (PDB: 3C6K). The pattern observed appears to correspond to a stratification of sectors where the N-terminal region associated with dimerization appears to dominate the red sector, whereas the C-terminal region, ranging from residues 173 to 366, is composed of the blue and green sectors. B) Distribution of the protein sectors in Rab GDP dissociation inhibitor. The analyzed residues correspond from positions 1 to 447 based on the PDB structure file (1LV0). The N-terminal FAD/NAD(P) binding domain appears to be predominantly composed of residues belonging to the green and blue sectors. The FAD-linked reductase and the C-terminal FAD/NAD(P) binding domains appear to have a majority of residues classified within the red sector with a small presence of amino acids belonging to the blue and green sectors.