id: Pfam:PF01345
pfam_id: PF01345
name: CLIPPER domain
short_name: CLIPPER
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01345
counters:
  proteins: 12543
  matches: 33340
  proteomes: 5220
  taxa: 8073
  structures: 1
  alphafold_models: 5072
  domain_architectures: 3336
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:IPR001434
description: This entry, previously known as DUF11, represents the CLIPPER domain, (Cross-Linked IsoPeptide
  Protein in the Extracellular Region) which is usually found in multiple copies in a number of archaebacterial
  proteins. CLIPPER domain adopts an Ig-like fold and contains a conserved N-terminal lysine and a C-terminal
  asparagine with central aspartate/glutamate residues that form an intramolecular isopeptide bond [[cite:PUB00163642]].
  The positions of the residues predicted to form isopeptide bonds are not universally conserved suggesting
  that some domains appear to lack the intramolecular isopeptide bonds. CLIPPER domains are found in proteins
  from Gram-positive and Gram-negative bacteria. Some have also been identified in multiple cell-surface
  proteins from archaea. In Methanothermobacter sp. CaT2, this domain plays a key role as a membrane-bound
  adhesion protein in the aggregation of CaT2 [[cite:PUB00097782]].