Structural comparison of orthologous proteins involved in vesicle trafficking.

<p>The structural characteristics of two orthologous protein pairs from the COPII vesicle trafficking system are presented. On panel A, the moderately disordered (34.13%) human Sec24A COPII adaptor subunit is compared to its virtually ordered (5.94%) yeast ortholog (SFB2, Sec24 related protein). On panel B, the highly disordered human Sec16A (71.41%) and yeast Sec16 (74.44%) proteins are presented. The disorder pattern predicted by the IUPred method is plotted for the members of each pair (blue curve), where the black dashed line (y = 0.5) represents the cut-off between order and disorder. Residues with disorder tendency above this cut-off are considered to be disordered. A domain map is also presented for each protein. In it, the location and names of their identified Pfam domains (gray segments) and their disordered binding regions predicted by the Anchor method (blue segments) are shown. In each panel, the human ortholog is depicted in the top part: the disorder prediction curve followed by its corresponding domain map. The bottom part of each panel is a specular representation of the corresponding yeast ortholog: the disorder curve is topped by the domain map. The corresponding disorder curves and domain maps are fitted in length so that structural information can be directly reflected on the disorder pattern. The blue dashed line connecting the domain maps in panel A shows the position in the human ortholog which corresponds to the N-terminal end of its yeast ortholog.