Protein Domain : Effector-associated domain 2 IPR045431

Type	Domain
Description	This entry represents the effector-associated domain 2 (EAD2). This domain is one of the most prevalent EADs, predominantly found in actinobacteria and to a lesser extent in cyanobacteria and Chloroflexi. EAD2 occurs fused to the signalling peptidases and nucleotide-utilizing domains fused to the VMAP component of those ternary systems and it has been suggested that it recruits the signalling components of the system []. It is predicted to be an all α-helical domain.Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteristic architectural pattern. One copy is always fused, typically to the N- or C-terminal, of a core component of a biological conflict system; examples include VMAP (vWA-MoxR associated protein), iSTAND (inactive STAND (iSTAND) NTPase system), or GAP1 (GTPase-associated protein 1). Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating EAD-EAD protein domain coupling approximates the advantages of collinear transcription [ , ]. EADs are all small domains with no enzymatic features.
Short Name	EAD2