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Eukaryotic organisms typically have many types of deubiquitinases, which differ in substrate specificity and the type of linkage of polyubiquitin chains [1]. Despite the high degree of structural variability of deubiquitinases, the catalytic domains of these enzymes are quite conservative. For example, all eukaryotic cysteine proteases have a characteristic papain-like fold [2]. In contrast to eukaryotes, the diversity of bacterial deubiquitinating enzymes is significantly reduced: globally, majority of bacterial deubiquitinases belong to either the OTU family or the CE-clan, which are also papain-like enzymes. [3]. Another difference between bacterial deubiquitinases is their narrower substrate specificity. Archaeal deubiquitinases belong to the JAMM family of metalloproteases and are similar to the eukaryotic deubiquitinase RPN11 [4]. Despite the obvious differences in the diversity and representation of various types of …