Charge distribution of the terminal domains of Y14. (A, upper panel) Domain organization of human Y14. (Lower panel) The structure of human Y14 was predicted by the AlphaFold Protein Structure network (https://github.com/deepmind/alphafold); the image was manipulated in PyMol Software (pymol.org). In all panels, acidic and basic residues are indicated in red and blue, respectively. RRM, RNA recognition motif; α0 and β0 represent the short α-helix and β-sheet, respectively. (B) Amino acid sequence alignment of human (Hs), Drosophila (Dm), and Caenorhabditis (Ce) Y14 homologs is shown according to a previous report (Fribourg et al. 2003). Conserved residues (identical or similar) in the amino-terminal domain are highlighted in gray. The two RS dipeptides in the carboxy-terminal domain of human Y14 are highlighted in yellow. (C) The amino- and carboxy-terminal domains of the three Y14 homologs in B were analyzed via Classification of Intrinsically Disordered Ensemble Regions (http://pappulab.wustl.edu/CIDER/analysis/). (NCPR) Net charge per residue distribution.
