In molecular biology, the EAL domain is a conserved protein domain. It is found in diverse bacterial signalling proteins, named EAL after its conserved residues. The EAL domain may function as a diguanylate phosphodiesterase. The domain contains many conserved acidic residues that can participate in metal binding and might form the phosphodiesterase active site. The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP [PMID: 15063857, PMID: 15289546, PMID: 15306016], and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria [PMID: 11557134].