id: Pfam:PF09189
pfam_id: PF09189
name: Archaeal MoaD-like protein
short_name: MoaD_arch
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09189
counters:
  proteins: 369
  matches: 371
  proteomes: 351
  taxa: 626
  structures: 1
  alphafold_models: 317
  domain_architectures: 3
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:IPR015272
description: This entry represents an archaeal MoaD-like domain with a ubiquitin-like fold found in various
  archaebacterial proteins. These proteins have a highly conserved Gly-Gly motif at their C-terminus,
  a hallmark of the MoaD/ThiS/ubiquitin superfamily [[cite:PUB00011756],[cite:PUB00035630]]. The bacterial
  MoaD protein functions as a sulfur carrier in molybdenum cofactor (Moco) biosynthesis, with the C-terminal
  Gly-Gly motif being essential for activation by the MoeB enzyme. After activation, MoaD receives a sulfur
  atom to form a thiocarboxylate intermediate that acts as a sulfur donor. Based on the conserved Gly-Gly
  motif and association with ThiS genes and MoaB-like proteins, these archaeal proteins likely function
  as sulfur carriers in cofactor biosynthesis pathways, similar to their bacterial counterparts.