id: Pfam:PF14487
pfam_id: PF14487
name: ssDNA thymidine ADP-ribosyltransferase, DarT
short_name: DarT
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF14487
counters:
  proteins: 1461
  matches: 1475
  proteomes: 1330
  taxa: 2780
  structures: 11
  alphafold_models: 881
  domain_architectures: 11
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:IPR029494
description: This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family
  are typically between 201 and 230 amino acids in length. There is a single completely conserved residue
  E that may be functionally important. This family is distantly similar to [pfam:PF01885]. Studies in
  search for novel ADP-ribosylation systems in bacterial genomes have identified an operon that encodes
  a conserved protein containing a distinct type of macrodomain associated with this family. This led
  to the identification of a toxin-antitoxin (TA) system, with DarT acting as the toxin. It is an enzyme
  that specifically modifies thymidines on single-stranded DNA in a sequence-specific manner by a nucleotide-type
  modification called ADP-ribosylation. This modification in turn can be removed by DarG, the antitoxin
  macrodomain protein. In addition, it was illustrated that substitution of the single completely conserved
  glutamate residue resulted in attenuation of function where DarT was non-toxic [[cite:PUB00091008]].