Protein Family Models

This domain, with its characteristic highly conserved CSS sequence motif, is found N-terminal to the EAL (Pfam:PF00563) domain in many cyclic diguanylate phosphodiesterases, such as PdeB/C/D/G/N from E. coli K-12 [1]. It has two highly conserved cysteine residues with potential disulfide bond formation, which might control the enzymatic activity of the cytoplasmic C-terminal EAL domain [1]. [1]. 29514851. Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase. Herbst S, Lorkowski M, Sarenko O, Nguyen TKL, Jaenicke T, Hengge R;. EMBO J. 2018; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function [1]. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site [1]. [1]. 11557134. Novel domains of the prokaryotic two-component signal transduction systems. Galperin MY, Nikolskaya AN, Koonin EV;. FEMS Microbiol Lett 2001;203:11-21. (from Pfam)

Date:

2024-10-16

cyclic di-GMP phosphodiesterase such as Escherichia coli PdeN, a phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG; includes Escherichia coli Rtn, which is involved in resistance to phages N4 and lambda

Date:

2018-08-24

Date:

2020-10-26