DBC1/CCAR2 and CCAR1 Are Largely Disordered Proteins that Have Evolved from One Common Ancestor

Figure 1

Disorder analysis shows the domain structure and molecular flexibility of hDBC1 and hCCAR1. The curves present the disorder score predicted by PONDR-FIT (FIT, dark cyan) and PONDR-VLXT (VLXT, dark pink). The -axis of human DBC1 (hDBC1, UniProtID: Q8N163) is shifted by 200 residues in order to align the C-terminus to human CCAR1 (hCCAR1, UniProtID: Q8IX12). The gray shadow behind PONDR-FIT represents the prediction of error. Residues with a score higher than 0.5 are disordered, while residues with a score lower than 0.5 are structured. The horizontal bars are the conserved functional domains identified in both proteins (S1-Like: aqua blue; NLS: medium blue; LZ: dark blue; Nudix: light purple; SAP: medium purple; CC1: dark purple; EF-Hand: light pink; CC2: dark pink). The predicted 3D structures are scaled roughly with their lengths.