|SMART accession number:||SM00951|
|Description:||QLQ is named after the conserved Gln, Leu, Gln motif. QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions (PUBMED:12974814).|
|Interpro abstract (IPR014978):|
The QLQ domain is characterised by the conserved Gln-Leu-Gln residues. Another feature of this domain is the absolute conservation of bulky aromatic/hydrophobic and acidic amino acid residues such as Phe, Trp, Tyr, Leu, Glu, or their equivalents in terms of chemical and radial properties. The Pro residue is also absolutely conserved. These amino acid residues are critical for the function of the QLQ domain, probably for protein-protein interaction [(PUBMED:12974814)].
Some proteins known to conatin a QLQ domain are listed below:
|GO process:||regulation of transcription, DNA-templated (GO:0006355)|
|GO component:||nucleus (GO:0005634)|
|GO function:||hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides (GO:0016818), ATP binding (GO:0005524)|
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Links (links to other resources describing this domain)