Extended Data Fig. 2: INP1 and INP2 proteins both contain the DOG1 domain and have similar structural organization predicted for their C-terminal parts.
From: A species-specific functional module controls formation of pollen apertures
a, Protein alignment between INP1 and INP2 proteins. Identical and similar (V/I/L, D/E, K/R, N/Q and S/T) residues are shaded, respectively, in blue and green. The positions of the DOG1 domains predicted by Pfam are indicated by purple lines. b-c, Protein structures predicted by Phyre2 for C-terminal parts of INP1 (b) and INP2 (c) (confidence: >97% for both proteins). In both cases, the modelled regions cover 114 amino acids, which constitute, respectively, 42% of INP1 and 37% of INP2. The same template (c4clvB, nickel-cobalt-cadmium resistance protein NccX from Cupriavidus metallidurans 31a) was selected by the program in both cases.
