id: Pfam:PF24346
pfam_id: PF24346
name: CLIPPER 2 domain
short_name: CLIPPER_2
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF24346
counters:
  proteins: 3311
  matches: 15693
  proteomes: 1861
  taxa: 3040
  structures: 0
  alphafold_models: 1164
  domain_architectures: 1301
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:IPR055354
description: This domain is found in multiple copies in a number of bacterial proteins. It is closely
  related to the CLIPPER domain ([pfam:PF01345]) and therefore it was named CLIPPER 2 (Cross-Linked IsoPeptide
  Protein in the Extracellular Region 2) [[cite:PUB00163642]]. Similarly to CLIPPER, this domain contains
  a conserved N-terminal lysine and a C-terminal asparagine with central aspartate/glutamate residues
  suggesting that it may contain an isopeptide bond. In addition, it contains a semi-conserved TNTGNV
  sequence motif in which a highly conserved asparagine probably plays a role in stabilising the rod structure
  formed by repetitive copies of this domain. Both CLIPPER and CLIPPER_2 domains are frequently found
  in tandem within surface polypeptides of bacteria and archaea, often alternating between the two families
  in tandem.