Fig. 3From: An OTU deubiquitinating enzyme in Eimeria tenella interacts with Eimeria tenella virus RDRPConserved sequence alignment of catalytic Cys, Asp and His residues of the OTU family of DUBs. Amino acid alignment of TgOTUD3A ( Toxoplasma gondii; GenBank: EPR62955.1), Otubain 2 (human; SW: Q96DC9), Otubain 1 (human; SW: Q96FW1), A20 (human; SW: P21580), Cezanne (human; SW: Q9NQ53) and VCIP135 (rat; SW: Q8CF97). The critical amino acid residues comprising the catalytic triad (Asp, Cys, and His) are highly conserved across these species (black asterisks) despite their evolutionary distance. The catalytic residues Asp, Cys, and His were mutated to generate Et-OTU (C239A), Et-OTU (D236A) and Et-OTU (H351A)Back to article page