HMM Summary Page: TIGR00254
Accession | TIGR00254 |
Name | GGDEF |
Function | diguanylate cyclase (GGDEF) domain |
Trusted Cutoff | 37.40 |
Domain Trusted Cutoff | 37.40 |
Noise Cutoff | 33.30 |
Domain Noise Cutoff | 33.30 |
Isology Type | domain |
HMM Length | 168 |
Mainrole Category | Regulatory functions |
Subrole Category | Small molecule interactions |
Gene Ontology Term | GO:0009966: regulation of signal transduction biological_process |
GO:0009975: cyclase activity molecular_function | |
Author | Haft DH |
Entry Date | Apr 20 1999 2:03PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity [1][3]. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus[2], and FixL, a heme-containing oxygen sensor protein. |
References | DR PFAM; PF00990; GGDEF RN [1] RM 11682196 RT Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. RL FEMS Microbiol Lett. 2001 Oct 16;204(1):163-7. RA Ausmees N, Mayer R, Weinhouse H, Volman G, Amikam D, Benziman M, Lindberg M. RN [2] RM 96042099 RT Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. RL J Bacteriol 1995 Nov;177(21):6223-9 RA Hecht GB, Newton A RN [3] RM 15306016 RT GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. RL Mol Microbiol. 2004 Aug;53(4):1123-34 RA Simm R, Morr M, Kader A, Nimtz M, Romling U RN [4] RM 15569936 RT Structural basis of activity and allosteric control of diguanylate cyclase. RA Chan C, Paul R, Samoray D, Amiot NC, Giese B, Jenal U, Schirmer T. RL Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17084-9 |