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PROSITE documentation PDOC50883 |
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.
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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). | |
PubMed ID | 9721278 |
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). | |
PubMed ID | 9537363 |
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). | |
PubMed ID | 11557134 |