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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the effector-associated domain 11 (EAD11). It is predicted to be an all α-helical domain [ ]. This domain is found in Roc-COR-CHAT protease, a recently characterised protease for substrate gasdermin bGSDM. It cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death [].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. | Name | Effector-associated domain 11 |
| Short Name | EAD11 | Type | Domain |
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