{PDOC51644}
{PS51644; HTH_OST}
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* OST-type HTH domain profile *
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The OST-HTH  (Oskar-TDRD5/TDRD7 HTH) [1] or LOTUS (after Limkain-b1, Oskar and
TUdor-containing proteins  5  and  7)  [2] domain is a motif of about 80 amino
acids and  is  likely to adopt a winged helix-turn-helix (wHTH) fold, which is
characterized by  a  core  3-stranded  HTH  with a C-terminal extension of two
strands. The OST-HTH domain is primarily found in eukaryotes and bacteria with
very rare  occurences  in  archaea  that  appear to be relatively late lateral
transfers of bacterial versions.

The OST-HTH  domain  is  likely  to  bind RNA with a potential specificity for
double-standed RNA  (dsRNA)  and  might  have  key  role  in  the assembly and
localization of  RNA-protein  complexes  with  important  post-transcriptional
regulatory functions.

Some proteins known to contain a OST-HTH domain are listed below:

 - Animal Limkain-b1 (LKAP).
 - Vertebrate Tudor domain-containing protein 5 (TDRD5), required during
   spermiogenesis to participate in the repression transposable elements and
   prevent their mobilization, which is essential for the germline integrity.
 - Vertebrate Tudor domain-containing protein 7 (TDRD7), probably acts by
   binding to specific mRNAs and regulating their translation.
 - Drosophila maternal effect protein oskar (osk), organizes the germ plasm
   and directs localization of the posterior determinant nanos.

The profile we developed covers the entire OST-HTH domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: May 2012 / First entry.

[ 1] Anantharaman V., Zhang D., Aravind L.
     "OST-HTH: a novel predicted RNA-binding domain."
     Biol. Direct 5:13-13(2010).
     PubMed=20302647; DOI=10.1186/1745-6150-5-13
[ 2] Callebaut I., Mornon J.P.
     "LOTUS, a new domain associated with small RNA pathways in the
     germline."
     Bioinformatics 26:1140-1144(2010).
     PubMed=20305267; DOI=10.1093/bioinformatics/btq122

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