{PDOC51793}
{PS51793; MIS18}
{BEGIN}
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* Mis18 domain profile *
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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 beta-strands  and a C-terminal alpha-helical domain. The oligomerization of
Mis18, mediated  by  its  conserved N-terminal globular domain, is crucial for
its centromere localization and function [1,2].

The Mis18  domain is mainly comprised of beta-strands (see <PDB:5HJ0>) 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 beta-sheets:  a  three stranded (beta1-beta2-beta9: beta-sheet I)
and a six stranded (beta3-beta4-beta8-beta7-beta6-beta5: beta-sheet II) sheet,
arranged approximately  perpendicular  to  each other. The two beta-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 [1,2].

The profile we developed covers the entire Mis18 domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2016 / First entry.

[ 1] Fujita Y., Hayashi T., Kiyomitsu T., Toyoda Y., Kokubu A., Obuse C.,
     Yanagida M.
     "Priming of centromere for CENP-A recruitment by human hMis18alpha,
     hMis18beta, and M18BP1."
     Dev. Cell 12:17-30(2007).
     PubMed=17199038; DOI=10.1016/j.devcel.2006.11.002
[ 2] Subramanian L., Medina-Pritchard B., Barton R., Spiller F.,
     Kulasegaran-Shylini R., Radaviciute G., Allshire R.C.,
     Arockia Jeyaprakash A.
     "Centromere localization and function of Mis18 requires Yippee-like
     domain-mediated oligomerization."
     EMBO Rep. 0:0-0(2016).
     PubMed=26921242; DOI=10.15252/embr.201541520

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