id: Pfam:PF20016
pfam_id: PF20016
name: Thoeris protein ThsA, Macro domain
short_name: ThsA_Macro
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF20016
counters:
  proteins: 534
  matches: 534
  proteomes: 453
  taxa: 1034
  structures: 5
  alphafold_models: 310
  domain_architectures: 9
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:IPR045535
description: Thoeris is a bacterial antiphage defense system, which consists of two genes, thsA and thsB,
  via NAD+ degradation [[cite:PUB00097806],[cite:PUB00101117],[cite:PUB00101118],[cite:PUB00160037]].
  ThsA has robust NAD+ cleavage activity and a two-domain architecture containing an N-terminal NAD-binding
  domain (denoted as sirtuin-like or Macro) and C-terminal SLOG-like domain. In some instances, such as
  in B. amyloliquefaciens ThsA has an N-terminal transmembrane domain [[cite:PUB00097806]]. ThsB (also
  referred to as TIR1 and TIR2) is structurally similar to TIR domain proteins but without enzymatic activity.
  This domain is found at the C-terminal of ThsA proteins which adopts a Rossmann-like fold that binds
  NAD+/NAD+derivatives. It has been characterised as the SLOG-like domain which binds NAD+ derivatives
  such as ADPR molecules produced by ThsB, which drives an oligomeric state change in ThsA and activates
  the NADase activity (represented in [pfam:PF18185]) [[cite:PUB00097806],[cite:PUB00101118]]. This entry
  represents the NAD+-binding Macro domain from B. amyloliquefaciens [[cite:PUB00097806],[cite:PUB00101117]].