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. Author manuscript; available in PMC: 2020 Jun 4.
Published in final edited form as: Structure. 2019 May 2;27(6):1000–1012.e6. doi: 10.1016/j.str.2019.03.022

Figure 1. Domain architecture of FAM105A and OTULIN.

Figure 1.

(A) FAM105A possesses an N-terminal predicted membrane localization motif (PMLM) and a C-terminal OTU domain. OTULIN possesses an N-terminal PUB interacting motif (PIM) and a C-terminal OTU domain. (B) Multiple sequence alignment of FAM105A and OTULIN from human, mouse, finch and Xenopus. Secondary structure elements are shown for FAM105A. Numbering refers to the human FAM105A and OTULIN sequences. Conserved residues are highlighted in grey. Residues comprising the linear diUb binding surface of OTULIN are highlighted in cyan in both OTULIN and FAM105A orthologues and red where divergent in FAM105A. Catalytic triad residues are indicated by red circles.