PROSITE documentation PDOC50887GGDEF domain profile
The GGDEF domain, which has been named after the conserved central sequence pattern GG[DE][DE]F is widespread in prokaryotes. It is typically present in multidomain proteins containing regulatory domains of signaling pathways or protein-protein or protein-ligand interaction modules, such as the response regulatory domain (see <PDOC50110)), the EAL domain (see <PDOC50883>), the PAS/PAC domain (see <PDOC50112>), the HAMP domain (see <PDOC50885>), the GAF domain, the FHA domain (see <PS50006>) or the TPR repeat. However a few single-domain proteins are also known. The GGDEF domain is involved in signal transduction and is likely to catalyze synthesis or hydrolysis of cyclic diguanylate (c-diGMP, bis(3',5')-cyclic diguanylic acid), an effector molecule that consists of two cGMP moieties bound head-to-tail [1,2,3].
Some proteins known to contain a GGDEF domain are listed below:
- Acetobacter xylinus diguanylate cyclases (DGCs) and c-di-GMP phosphodiesterases A (PDEAs).
- Bacillus subtilis hypothetical protein yhcK.
- Caulobacter crescentus pleD protein, a response regulator that controls cell differentiation in the swarmer-to-stalked cell transition.
- Rhizobium celR2, a putative response regulator protein.
- Salmonella protein adrA.
The profile we developed covers the entire GGDEF domain.
Last update:February 2003 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | 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 |
2 | Authors | Ausmees N. Mayer R. Weinhouse H. Volman G. Amikam D. Benziman M. Lindberg M. |
Title | Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. | |
Source | FEMS Microbiol. Lett. 204:163-167(2001). | |
PubMed ID | 11682196 |
3 | Authors | Pei J. Grishin N.V. |
Title | GGDEF domain is homologous to adenylyl cyclase. | |
Source | Proteins 42:210-216(2001). | |
PubMed ID | 11119645 |
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