{PDOC51848} {PS51848; BMERB} {BEGIN} ************************ * bMERB domain profile * ************************ A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The "bivalent Mical/EHBP Rab binding" (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element [1]. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix (see ) [1]. Some proteins known to contain a bMERB domain are listed below: - Animal proteins of the Molecules Interacting with CasL (Mical) family, multidomain, mainly cytoplasmic, proteins, which participate in the control of actin cytoskeleton dynamics. - Animal Eps15-homolgy (EH) domain binding proteins (EHBPs), couple vesicular transport to the actin cytoskeleton. - Animal C16orf45 proteins. The profile we developed covers the entire bMERB domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: November 2017 / First entry. [ 1] Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S., Gazdag E.M., Muller M.P. "bMERB domains are bivalent Rab8 family effectors evolved by gene duplication." Elife 5:0-0(2016). PubMed=27552051; DOI=10.7554/eLife.18675 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}