id: Pfam:PF05639
pfam_id: PF05639
name: Pup-like protein
short_name: Pup
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05639
counters:
  proteins: 3495
  matches: 3495
  proteomes: 3401
  taxa: 4136
  structures: 12
  alphafold_models: 2101
  domain_architectures: 4
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:IPR008515
description: This family consists of several short bacterial proteins formely known as (DUF797). It was
  recently shown that Mycobacterium tuberculosis contains a small protein, Pup (Rv2111c), that is covalently
  conjugated to the e-NH2 groups of lysines on several target proteins (pupylation) such as the malonyl
  CoA acyl carrier protein (FabD) [[cite:PUB00053383]]. Pupylation of FabD was shown to result in its
  recruitment to the mycobacterial proteasome and subsequent degradation analogous to eukaryotic ubiquitin-conjugated
  proteins. Searches recovered Pup orthologs in all major actinobacteria lineages including the basal
  bifidobacteria and also sporadically in certain other bacterial lineages. [[cite:PUB00053382]] The Pup
  proteins were all between 50-90 residues in length and a multiple alignment shows that they all contain
  a conserved motif with a G [EQ] signature at the C-terminus. Thus, all of them are suitable for conjugation
  via the terminal glutamate or the deamidated glutamine (as shown in the case of the Mycobacterium Pup
  [[cite:PUB00053382]]). The conserved globular core of Pup is predicted to form a bihelical unit with
  the extreme C-terminal 6-7 residues forming a tail in the extended conformation. Thus, Pup is structurally
  unrelated to the ubiquitin fold and has convergently evolved the function of protein modifier.