Protein Domain : Effector-associated domain 1 IPR045430

Type	Domain
Description	This entry represents the effector-associated domain 1 (EAD1). This domain is one of the most prevalent EADs, widely distributed across bacteria. EAD1 is primarily linked to effector domains that also occur directly fused to the vWA component in MoxR-vWA ternary systems or GAP1 in the case of the GAP1-N1 GTPases systems which suggests that it primarily recruits other effectors to the systems [ ]. 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	EAD1