Protein Domain : Mis18 domain IPR034752

Type	Domain
Description	The centromere is the chromosomal site that joins to microtubules during mitosis for proper segregation. Centromere protein A (CENP-A) is a histone H3 variant and an essential component of centromeres. Mis18 proteins are involved in the priming of centromeres for recruitment of CENP-A. They possess two structurally distinct domains: an N-terminal globular domain mainly comprised of β-strands and a C-terminal α-helical domain. The oligomerization of Mis18, mediated by its conserved N-terminal globular domain, is crucial for its centromere localization and function [ , ].The Mis18 domain is mainly comprised of β-strands and has two conserved C-x-x-C motifs, which are signatures motifs present in metal ion-binding proteins. The overall fold of the Mis18 domain is formed by antiparallel β-sheets: a three stranded (β1-β2-β9: β-sheet I)and a six stranded (β3-β4-β8-β7-β6-βa5: β-sheet II) sheet, arranged approximately perpendicular to each other. The two β-sheets are held together by a Zn(2+) ion coordinated via the C-x-x-C motifs from loops L1 and L5. The Mis18 domain contains a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which is required for Mis18 function [, ].
Short Name	Mis18