id: Pfam:PF06114
pfam_id: PF06114
name: IrrE N-terminal-like domain
short_name: Peptidase_M78
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06114
counters:
  proteins: 21240
  matches: 21261
  proteomes: 11259
  taxa: 16625
  structures: 10
  alphafold_models: 13293
  domain_architectures: 143
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:IPR010359
description: This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase
  containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon.
  Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance
  to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself
  and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative
  tranposon encodes only the proteins required for this activity and the proteins that regulate it. During
  exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor
  protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer.
  Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be
  essential for the cleavage of ImmR [[cite:PUB00066798]]. This domain is also found in in metalloprotease
  IrrE, a central regulator of DNA damage repair in Deinococcaceae [[cite:PUB00051490]], HTH-type transcriptional
  regulators RamB [[cite:PUB00074928]] and PrpC [[cite:PUB00074929]].