PROSITE documentation PDOC51644OST-type HTH domain profile
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.
Last update:May 2012 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Anantharaman V. Zhang D. Aravind L. |
| Title | OST-HTH: a novel predicted RNA-binding domain. | |
| Source | Biol. Direct 5:13-13(2010). | |
| PubMed ID | 20302647 | |
| DOI | 10.1186/1745-6150-5-13 |
| 2 | Authors | Callebaut I. Mornon J.P. |
| Title | LOTUS, a new domain associated with small RNA pathways in the germline. | |
| Source | Bioinformatics 26:1140-1144(2010). | |
| PubMed ID | 20305267 | |
| DOI | 10.1093/bioinformatics/btq122 |
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