Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51708CHAD domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51708
The CHAD (conserved histidine α-helical domain) is an uncharacterized domain, with a characteristic pattern of conserved histidines and other charged residues. It is predicted to adopt an α-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 [1].
Some proteins known to contain a CHAD domain are listed below:
- Escherichia coli uncharacterized protein YgiF.
- Mycobacterium tuberculosis uncharacterized protein Rv2226/MT2285.
The profile we developed covers the entire CHAD domain.
Last update:February 2014 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Iyer L.M. Aravind L. |
| Title | The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates. | |
| Source | BMC Genomics 3:33-33(2002). | |
| PubMed ID | 12456267 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.