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C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar proteins Wip1, also called CENP-W homolog, or constitutive centromere-associated network protein Wip1, is a component of the inner kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. The model corresponds to the C-terminal histone fold domain of Wip1, which interacts with Cnn1 to form a heterodimer. In budding yeast, the Cnn1-Wip1 heterodimer associated with the Ctf3 complex (Ctf3c) to form a sub-complex of the larger Ctf19 complex (Ctf19c).
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Jiyao W et al.(2023). "The conserved domain database in 2023.",