|SMART accession number:||SM00880|
|Description:||The CHAD domain is an alpha-helical domain functionally associated with some members of the adenylate cyclase family . It has conserved histidines that may chelate metals.|
|Interpro abstract (IPR007899):|
The CHAD (conserved histidine alpha-helical domain) is an uncharacterised domain, with a characteristic pattern of conserved histidines and other charged residues. It is predicted to adopt an alpha-helical fold. The sequence conservation pattern suggests that this domain is likely to contain two repeat units, with at least 4 helices each, at its core. The conserved charged residues could form a strongly polar surface that could participate, either in metal chelation, or act as phosphoacceptors [(PUBMED:12456267)].
Some proteins known to contain a CHAD domain are listed below:
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)