Fig. 3: Identification of Mn repeats in eukaryotic MIPs. | Nature Communications

Fig. 3: Identification of Mn repeats in eukaryotic MIPs.

From: Uncovering structural themes across cilia microtubule inner proteins with implications for human cilia function

Fig. 3

a Multiple sequence alignment of the Mn repeat units from human proteins identified by iterative HMM-to-HMM searches. The expanded alignment with C. reinhardtii Mn repeat proteins is shown in supplementary Fig. S2c. Proteins are designated by their UniProt identifiers. Coloring schemes as per ClustalX parameters with modifications. Shown in green are positions where hydrophilicity and aromatic residues are conserved and participate in the short α-helix of individual Mn repeat unit. Predicted regions corresponding to α-helices and based on FAP363 Mn repeats, are shown above the alignment. b Portions of the elongated Mn repeat proteins SAXO1, SAXO2, and TEX26 as predicted by comparative modeling as well as deep learning by AlphaFold2. c Module architecture of proteins with known and predicted Mn repeats and inferred Mn repeat. d Superimposed Mn repeat units of human CFAP95, CFAP107, and SPAG8as assessed by Pymol. e Examples of Mn repeat unit contact sites with the MT lattice in mammals. The Mn unit is shown in green, and MT contact side chains are shown in red.

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