|PROSITE documentation PDOC50883 [for PROSITE entry PS50883]|
The EAL domain is an around 250-amino acid signaling domain. It is made of four conserved regions and has been named EAL according to a conserved sequence within the second of these regions. The EAL domain is found in a large number of eubacterial multi-domain proteins involved in signal transduction. The EAL domain is found in association with other domains of the prokaryotic two-component signal transduction systems, such as the GGDEF domain (see <PDOC50887>), the response regulatory domain (see <PDOC50110>), the PAS repeat and the PAC domain (see <PDOC50112>), the MHYT domain, the HAMP domain (see <PDOC50885>), the GAF domain, the TPR repeat, or the FHA domain (see <PDOC50006>). It has been proposed that the EAL domain might function as a diguanylate phosphodiesterase. Accordingly, it contains several conserved acidic residues that could participate in metal binding and potentially might form a phosphodiesterase active site [1,2,3].
Some proteins known to contain an EAL domain are listed below:
The profile we developed covers the entire EAL domain.Last update:
December 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Tal R., Wong H.C., Calhoon R., Gelfand D., Fear A.L., Volman G., Mayer R., Ross P., Amikam D., Weinhouse H., Cohen A., Sapir S., Ohana P., Benziman M.|
|Title||Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes.|
|Source||J. Bacteriol. 180:4416-4425(1998).|
|2||Authors||Merkel T.J., Barros C., Stibitz S.|
|Title||Characterization of the bvgR locus of Bordetella pertussis.|
|Source||J. Bacteriol. 180:1682-1690(1998).|
|3||Authors||Galperin M.Y., Nikolskaya A.N., Koonin E.V.|
|Title||Novel domains of the prokaryotic two-component signal transduction systems.|
|Source||FEMS Microbiol. Lett. 203:11-21(2001).|