SMART: Pfam domain OST-HTH

The domain within your query sequence starts at position 1483 and ends at position 1555; the E-value for the OST-HTH domain shown below is 3e-14.

TSLYLFAKNVRSLLHTYHYQQIFLHEFSMAYNKYVGETLQPKTYGYSSVEELLGAIPQVV
WIKGHGHKRIVVL

OST-HTH

PFAM accession number:	PF12872
Interpro abstract (IPR025605):	This predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organise structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood [ (PUBMED:20302647) (PUBMED:20305267) ]. The domain adopts the winged helix-turn-helix fold and binds RNA with a potential specificity for dsRNA [ (PUBMED:20302647) ]. In eukaryotes, this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localisation of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains, indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterised RNAse domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains [ (PUBMED:20302647) ].

PFAM accession number:

PF12872

Interpro abstract (IPR025605):

This predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organise structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood [ (PUBMED:20302647) (PUBMED:20305267) ]. The domain adopts the winged helix-turn-helix fold and binds RNA with a potential specificity for dsRNA [ (PUBMED:20302647) ]. In eukaryotes, this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localisation of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains, indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterised RNAse domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains [ (PUBMED:20302647) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry OST-HTH