id: Pfam:PF12130
pfam_id: PF12130
name: Bivalent Mical/EHBP Rab binding domain
short_name: bMERB_dom
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12130
counters:
  proteins: 12866
  matches: 13023
  proteomes: 1275
  taxa: 4099
  structures: 14
  alphafold_models: 7449
  domain_architectures: 118
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR022735
description: 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. 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 [[cite:PUB00088663]].