id: Pfam:PF01934
pfam_id: PF01934
name: Ribonuclease HepT-like
short_name: HepT-like
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01934
counters:
  proteins: 7949
  matches: 7950
  proteomes: 4926
  taxa: 8359
  structures: 11
  alphafold_models: 5432
  domain_architectures: 17
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:IPR008201
description: This family includes the toxic component HepT of a type II toxin-antitoxin (TA) system, which
  has RNase activity. These proteins contain a HEPN (higher eukaryotes and prokaryotes nucleotide-binding)
  domain and are neutralised through tri-AMPylation by the cognate antitoxin MntA, containing a MNT (minimal
  nucleotidyltransferase) domain [[cite:PUB00097221],[cite:PUB00097219],[cite:PUB00097220]]. HepT-MnA
  form an heterooctamer (at a 2:6 ratio), a rare organisation for this kind of TA systems. HepT dimerises
  and enables the formation of a deep cleft at the HEPN-domain interface, containing the RX4-6H motif
  (where X is any amino acid and the residue immediately after the conserved R is typically a polar amino
  acid) as the active site that functions as an RNA-cleaving RNase. This type II TA system regulates cell
  motility and confers plasmid stability [[cite:PUB00097219]]. Due to the prevalence of these HEPN/MNT
  modules in bacteria and archaea, it has been suggested that these TA systems may also play a role in
  the environmental adaptation to extreme habitats [[cite:PUB00097220]].