Fig. 1.

Sequence alignments and structural predictions for CinB. (A) The NTND and CTND of CinB^wPip with their predicted catalytic aspartate, glutamate, and lysine residues labeled. CidB^wPip also has 2 predicted PD-(D/E)xK nuclease folds upstream of its deubiquitylase domain; these are related to the dual nuclease domains in CinB^wPip but lack 2 or 3 of the 3 predicted core catalytic residues. (B) Protein sequence and secondary structure alignments of the NTND and CTND of CinB from various Wolbachia strains as well as several known PD-(D/E)xK nucleases. Predicted α-helical residues are labeled “H” and residues predicted to be part of β-sheets are labeled “E.” The numbers of excluded residues are shown in parentheses. The last residue numbers are shown at the end of each sequence. Catalytic D-E-K residues are highlighted in black. Residues in red are conserved among all 3 groups. Residues in gray are conserved within the respective groups.