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. 2017 Jun 19;26(9):1870–1877. doi: 10.1002/pro.3210

Figure 2.

Figure 2

Comparison of human WBSCR16 with RCC1 and other RCC1‐like proteins. (A) Multiple sequence alignment of human WBSCR16, human RCC1, yeast Prp20p, human RPGR, and the third RCC1‐like domain of human HERC1. Similarity scores were calculated using the ENDscript web server, according to a matrix based on physicochemical properties. Residue names are written in black if score is below 0.7 (low similarity); they are in red on a yellow background if score is in the range 0.7–1 (high similarity); they are in white on a red background in case of strict identity. The positions of β‐strands of WBSCR16 are indicated by arrows above the sequence. Solvent accessibility of WBSCR16 residues is rendered by a bar below the sequence (blue is accessible, cyan is intermediate, white is buried) (B) Stereoview of a sausage drawing of WBSCR16. For this drawing, the structures of human RCC1 (PDB code, 1I2M, chain B), yeast Prp20p (PDB code, 3OF7, chain A), human RPGR (PDB code, 4JHP, chain C), and the third RCC1‐like domain of human HERC1 (PDB code, 4O2W, chain A) were superposed onto the structure of human WBSCR16, and the radius of the sausage is proportional to the mean r.m.s.d. per residue between Cα pairs. To visualize sequence conservation, the sausage is color ramped from white [similarity score calculated in (A) below 0.7] to red (strict identity).