Protein Family Models

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-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. 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 the EAD-EAD coupling approximates the advantages of collinear transcription. Profile-profile searches unify EAD2 with the Death superfamily of domains [2]. [1]. 32101166. Highly regulated, diversifying NTP-dependent biological conflict systems with implications for the emergence of multicellularity. Kaur G, Burroughs AM, Iyer LM, Aravind L;. Elife. 2020; [Epub ahead of print]. [2]. 34061031. Bacterial death and TRADD-N domains help define novel apoptosis and immunity mechanisms shared by prokaryotes and metazoans. Kaur G, Iyer LM, Burroughs AM, Aravind L;. Elife. 2021; [Epub ahead of print] (from Pfam)

Date:

2024-11-04

Highly variable central region of the vWA-MoxR associated protein (VMAP) of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. VMAP-Ms may be involved in sensing of invasive entities. [1]. 32101166. Highly regulated, diversifying NTP-dependent biological conflict systems with implications for the emergence of multicellularity. Kaur G, Burroughs AM, Iyer LM, Aravind L;. Elife. 2020; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

C-terminal region of the VMAP protein of the classical ternary system (vWA-MoxR-VMAP) in NTP-dependent conflict systems. Mixed alpha+beta domain with no apparent structural similarity to known protein folds. Contains several, nearly universally polar residues, suggesting a conserved interaction interface. Enzymatic function for VMAP-C though possible appears unlikely. Sensing of invasive elements by VMAP-Ms are predicted to trigger a sequence of conformational changes, which is communicated to the switch-component (MoxR) of the system via the more constant VMAP-C [1]. [1]. 32101166. Highly regulated, diversifying NTP-dependent biological conflict systems with implications for the emergence of multicellularity. Kaur G, Burroughs AM, Iyer LM, Aravind L;. Elife. 2020; [Epub ahead of print] (from Pfam)

Date:

2024-10-16