{PDOC51913}
{PS51913; HTH_HARE}
{BEGIN}
********************************
* HARE-type HTH domain profile *
********************************

Human ASXL  proteins,  orthologs of Drosophila Additional Sex combs, have been
implicated in  conjunction  with  TET2  as  a  major  target for mutations and
translocations leading   to   a  wide  range  of  myeloid  leukemias,  related
myelodysplastic conditions (ASXL1 and ASXL2) and the Bohring-Opitz syndrome, a
developmental disorder   (ASXL1).   Most  animal  ASXL  proteins  (except  the
Drosophila Asx  protein)  contain  an  N-terminal domain that is also found in
several other  eukaryotic  chromatin  proteins  (including  Arabidopsis  HB1),
diverse restriction  endonucleases  and  DNA  glycosylases, the RNA polymerase
delta subunit  of  Gram-positive  bacteria and certain bacterial proteins that
combine features  of  the RNA polymerase alpha-subunit and sigma factors. This
domain adopts  the  winged helix-turn-helix fold and is predicted to bind DNA.
It has  been  named  HARE-type  HTH,  for HB1, ASXL, restriction endonuclease,
based on the proteins in which it was detected [1,2].

The HARE-type  HTH  domain consists of four alpha-helices (helices I, II, III,
and IV) and an antiparallel beta-sheet composed of three short beta-strands at
the top  of  a  "twisted  tripod"  formed  by  helices  II,  III,  and IV (see
<PDB:2KRC>) [2].

The profile we developed covers the entire HARE-type HTH domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2020 / First entry.

[ 1] Aravind L., Iyer L.M.
     "The HARE-HTH and associated domains: novel modules in the
     coordination of epigenetic DNA and protein modifications."
     Cell. Cycle. 11:119-131(2012).
     PubMed=22186017; DOI=10.4161/cc.11.1.18475
[ 2] Motackova V., Sanderova H., Zidek L., Novacek J., Padrta P.,
     Svenkova A., Korelusova J., Jonak J., Krasny L., Sklenar V.
     "Solution structure of the N-terminal domain of Bacillus subtilis
     delta subunit of RNA polymerase and its classification based on
     structural homologs."
     Proteins 78:1807-1810(2010).
     PubMed=20310067; DOI=10.1002/prot.22708

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}