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AlphaFold-guided structural analysis not only confirmed functional orthologues found across eukaryotes, but also identified apicomplexan-specific enzymes, subsequently enabling discovery of a cryptic OTU DUB in\n                    <jats:italic>Plasmodium<\/jats:italic>\n                    species. Comprehensive biochemical characterisation of 11\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    OTU DUBs revealed activity against ubiquitin- and NEDD8-based substrates and revealed ubiquitin linkage preferences for Lys6-, Lys11-, Lys48-, and Lys63-linked chain types. We show that accessory domains in\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    OTU DUBs impose linkage preferences, and in case of apicomplexan-specific TgOTU9, we discover a cryptic ubiquitin-binding domain that is essential for TgOTU9 activity. Using the auxin-inducible degron (AID) to generate knockdown parasite lines, TgOTUD6B was found to be important for\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    growth.\n                  <\/jats:p>","DOI":"10.26508\/lsa.202201710","type":"journal-article","created":{"date-parts":[[2023,3,23]],"date-time":"2023-03-23T15:25:20Z","timestamp":1679585120000},"page":"e202201710","update-policy":"https:\/\/doi.org\/10.26508\/lsa.crossmarkpolicy","source":"Crossref","is-referenced-by-count":10,"title":["Characterisation of the OTU domain deubiquitinase complement of\n                    <i>Toxoplasma gondii<\/i>"],"prefix":"10.26508","volume":"6","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0528-392X","authenticated-orcid":true,"given":"Mary-Louise","family":"Wilde","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01b6kha49","id-type":"ROR","asserted-by":"publisher"}],"name":"Walter and Eliza Hall Institute of Medical Research","place":[", Parkville, Australia; 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