Dag system

traitmech:000507 · CLASS · PROPOSED

A phage defense system in which an organism possesses a Dag-family DNA-glycosylase system whose Dag1 or Dag2 effectors selectively target phages carrying modified guanine bases.

Trait evidence (4)

DOI:10.1038/s41564-026-02441-0
using structure-guided discovery, we identified two widespread families of anti-phage DNA glycosylases, Dag1 and Dag2

Getz et al. identify Dag1 and Dag2 as widespread anti-phage DNA-glycosylase families.
DOI:10.1038/s41564-026-02441-0
Dag1 and Dag2 act as antiviral effectors that selectively target phages carrying modified guanine bases.

Getz et al. support the modified-guanine phage targeting scope of the Dag1 and Dag2 antiviral effectors.
DOI:10.1038/s41564-026-02441-0
Together, these findings establish DNA glycosylases as a versatile class of bacterial immune proteins

Getz et al. frame defense-associated DNA glycosylases as bacterial immune proteins.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md
| Dag | 10\.1101/2025\.10\.29\.685425 | Antiviral defence is a conserved function of diverse DNA glycosylases |

The pinned DefenseFinder article registry maps the Dag source key to the Getz et al. DNA-glycosylase antiviral defense paper.

Dag effectors target modified-guanine phages

Conservative system-level sketch linking the Dag DefenseFinder namespace to Dag1 and Dag2 antiviral effector activity and the Dag phage-defense-system trait.

NONMECHANISTIC · The graph captures Dag as a named DefenseFinder DNA-glycosylase phage-defense system at system level and deliberately defers a protein-resolved glycosylase mechanism. Getz et al. support Dag1 and Dag2 as anti-phage DNA glycosylase families that target modified-guanine phages, but exact natural host exemplars, accession-level Dag proteins, relationships between Dag1 and Dag2 families, and DefenseFinder HMM/rules profiles are unresolved.

Edge evidence

Dag locus contributes to modified-guanine phage targeting RO:0002326
Dag-family DNA-glycosylase systems encode Dag1 or Dag2 antiviral effectors that selectively target modified-guanine phages.
- DOI:10.1038/s41564-026-02441-0 using structure-guided discovery, we identified two widespread families of anti-phage DNA glycosylases, Dag1 and Dag2 Getz et al. identify Dag1 and Dag2 as widespread anti-phage DNA-glycosylase families.
- DOI:10.1038/s41564-026-02441-0 Dag1 and Dag2 act as antiviral effectors that selectively target phages carrying modified guanine bases. Getz et al. support the modified-guanine phage targeting scope of the Dag1 and Dag2 antiviral effectors.
- https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md | Dag | 10\.1101/2025\.10\.29\.685425 | Antiviral defence is a conserved function of diverse DNA glycosylases | The pinned DefenseFinder article registry maps the Dag source key to the Getz et al. DNA-glycosylase antiviral defense paper.
modified-guanine phage targeting confers Dag system METPO:2007700
Modified-guanine phage targeting realizes the organism-level Dag system possession trait.
- DOI:10.1038/s41564-026-02441-0 Dag1 and Dag2 act as antiviral effectors that selectively target phages carrying modified guanine bases. Getz et al. support the modified-guanine phage targeting scope of the Dag1 and Dag2 antiviral effectors.
- DOI:10.1038/s41564-026-02441-0 Together, these findings establish DNA glycosylases as a versatile class of bacterial immune proteins Getz et al. frame defense-associated DNA glycosylases as bacterial immune proteins.
Dag system is a phage defense system rdfs:subClassOf
Dag system possession is a phage-defense-system trait.
- DOI:10.1038/s41564-026-02441-0 using structure-guided discovery, we identified two widespread families of anti-phage DNA glycosylases, Dag1 and Dag2 Getz et al. identify Dag1 and Dag2 as widespread anti-phage DNA-glycosylase families.
- DOI:10.1038/s41564-026-02441-0 Together, these findings establish DNA glycosylases as a versatile class of bacterial immune proteins Getz et al. frame defense-associated DNA glycosylases as bacterial immune proteins.

Provenance

Identifier source: TraitMech local identifier
Definition source: DOI:10.1038/s41564-026-02441-0

Parent traits (1)

phage defense system traitmech:000209

Synonyms (3)

Dag RELATED_SYNONYM · https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md
Dag1 RELATED_SYNONYM · DOI:10.1038/s41564-026-02441-0
Dag2 RELATED_SYNONYM · DOI:10.1038/s41564-026-02441-0

kg-microbe context

No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.

Discussions and Knowledge Gaps (1)

Open questions attached to this trait. Seeded by just knowledge-gap-scan and curated; see the corpus-wide index.

Resolve exact Dag1 and Dag2 family boundaries, natural host exemplars, modified-guanine phage target breadth, and DefenseFinder HMM/rules coverage before minting narrower Dag mechanism or component traits.

KNOWLEDGE GAP OPEN dag-defensefinder-profile-gap · raised by codex · 2026-10-01

Attached to causal_graphs#dag_effectors_target_modified_guanine_phages

Getz et al. support Dag1 and Dag2 as widespread families of anti-phage DNA glycosylases that selectively target phages carrying modified guanine bases, and the pinned DefenseFinder article registry maps the Dag key to the Getz et al. preprint DOI. The pinned HMM inventory and rules table have no exact Dag rows. This first-pass record therefore does not resolve exact Dag1 versus Dag2 family boundaries, natural host exemplars, accession-level Dag proteins, full modified-guanine phage target breadth, or a reusable DefenseFinder profile model.

Evidence

DOI:10.1038/s41564-026-02441-0
using structure-guided discovery, we identified two widespread families of anti-phage DNA glycosylases, Dag1 and Dag2
DOI:10.1038/s41564-026-02441-0
Dag1 and Dag2 act as antiviral effectors that selectively target phages carrying modified guanine bases.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md
| Dag | 10\.1101/2025\.10\.29\.685425 | Antiviral defence is a conserved function of diverse DNA glycosylases |
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv

Curation history

2026-10-01T05:07:00Z · MINTED_TRAITMECH_ID · codex
Minted Dag system as a DOI- and DefenseFinder-backed GENOMICS TraitRecord under the phage defense system parent after an ignored-and-hidden duplicate review found no exact live TraitMech, METPO, history, or prior proposal record; the replacement placeholder is reserved in proposals/metpo_traitmech_v384.
2026-10-01T05:07:01Z · REVIEW_CANONICAL_EXAMPLE_EVIDENCE_GAP · codex
Reviewed Dag system during initial curation and left canonical_examples empty because the accessible Getz et al. abstract supports Dag1 and Dag2 as widespread anti-phage DNA-glycosylase families but does not name a stable NCBITaxon strain exemplar for the organism-level Dag system trait. No paid research was used.