id: Pfam:PF01661
pfam_id: PF01661
name: Macro domain
short_name: Macro
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01661
counters:
  proteins: 32372
  matches: 38291
  proteomes: 12852
  taxa: 24044
  structures: 1152
  alphafold_models: 21017
  domain_architectures: 1119
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:IPR002589
description: 'The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose
  (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent
  [[cite:PUB00052327]]: in certain cases it is believed to bind non-covalently [[cite:PUB00052325]]; while
  in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif,
  and covalently through a separate region of the protein [[cite:PUB00052328]]. This domain is found in
  a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein
  4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses
  and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria
  and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting
  of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face,
  and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms
  the C terminus of the protein [[cite:PUB00043976]]. The crystal structure of AF1521 (a Macro domain-only
  protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing
  proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the
  first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic
  cleft and cluster around the AF1521-ADP-ribose binding site [[cite:PUB00021744]].'