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(C) Table showing the E-values and percent identities of TTHERM_00382220 and TTHERM_00194700 aligned to the human CPAP protein sequence. thermophila Im, Ichthyophthirius multifiliis Pt, Paramecium tetraurelia Cr, Chlamydomonas reinhardtii. Dm, Drosophila melanogaster Mm, Mus musculus Dr, Danio rerio Xl, Xenopus laevis Hs, Homo sapiens Sp, Strongylocentrotus purpuratus Tt, T. This supports the hypothesis that TTHERM_00382220 is a Sas4 homologue and that TTHERM_00194700 is not likely a true Sas4 homologue or a paralog to TTHERM_00382220. The phylogenetic tree shows that the TTHERM_00194700 and Pt_00194700-like proteins cluster together and are distantly related to the Paramecium Sas4 proteins. BLAST analysis of the TTHERM_00194700 protein sequence in the Paramecium genome revealed two additional Paramecium genes, which we identify as Pt_00194700-like(L). Phylogenetic tree was created using in one-click mode. The SAS4 gene described in this paper (TTHERM_00382220) is closely related to the three previously studied Paramecium SAS4 paralogs, whereas TTHERM_00194700 is distantly related. (B) Phylogenetic analysis of Sas4 proteins, known and predicted (indicated by “pred.”). Enlarged panel is rotated 90° counter-clockwise and shows weak cortical row and cilia localization. (A) Endogenous TTHERM_00194700:HaloTag (grayscale) localizes to oral apparatus and oral primordium cilia, cortical cilia, and to cortical rows. Thus, Sas4 links BBs with an ancient signaling pathway known to promote the accurate and symmetric segregation of the genome. We find that Sas4 loss disrupts localization of the Hippo activator, Mob1, suggesting that Sas4 mediates Hippo activity by promoting scaffolds for Mob1 localization to the cell cortex. The Hippo signaling pathway is known to regulate cell division furrow position, and Hippo molecules localize to BBs and BB-appendages. Sas4 is necessary for BB assembly and cortical microtubule organization, and Sas4 loss disrupts cell division furrow positioning and DNA segregation. The Tetrahymena Sas4/CPAP protein is enriched at assembling BBs, localizing to the core BB structure and to the base of BB-appendage microtubules and striated fiber. Both BB assembly and DNA replication are tightly coordinated with the cell cycle to ensure their accurate segregation and propagation to daughter cells, but the mechanisms ensuring coordination are unclear. Basal bodies (BBs) are macromolecular complexes required for the formation and cortical positioning of cilia.