id: Pfam:PF11962
pfam_id: PF11962
name: Peptidase_G2, IMC autoproteolytic cleavage domain
short_name: Peptidase_G2
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11962
counters:
  proteins: 321
  matches: 340
  proteomes: 241
  taxa: 502
  structures: 11
  alphafold_models: 163
  domain_architectures: 31
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:IPR021865
description: This domain is found at the very C-terminus of bacteriophage parallel beta-helical tailspike
  proteins. It carries the enzymic residues that induce autoproteolytic cleavage to bring about maturation
  of the folding process of the helix in a chaperone-like manner. The domain thus mediates the assembly
  of a large tailspike protein and then releases itself after maturation. These C-terminal regions that
  autoproteolytically release themselves after maturation are exchangeable between functionally unrelated
  N-terminal proteins and have been identified in a number of bacteriophage tailspike proteins [[cite:PUB00057232]].