Fig. 5
From: Population genetics of Babesia vogeli based on the mitochondrial cytochrome b gene
Protein characteristics and homology modeling of the partial cyt b protein of B. vogeli. (a) Secondary structure of 228 amino acids cyt b protein contained nine alpha helices (red; numbered in green) as predicted by PSIPRED. (b) Surface clefts are depicted as solid-coloured regions according to volume, with the largest shown in red, and it represents the protein's binding site. (c) It is composed of three extracellular domains (1R-A5, 51G-I97, and 164I-L207,), five transmembrane domains (6Q-W24, 33S-L50, 98L-L117, 141 V-G163 and 208A-V224) and three cytoplasmic domains (25Y-W32, 118H-V140 and 225E-A228). (d) Ribbon representation of homology model of the cyt b protein produced using automated homology prediction by SWISS-MODEL server by utilizing the cytochrome b protein of B. gibsoni (UniProt ID—A0A649UJK2) as template. Alpha helices and loops/coils are represented in red and green colors, respectively. The abbreviations used are as follows: α, alpha helix; N – N-terminus; C – C-terminus.
