Avs IV system
traitmech:000537 · CLASS · PROPOSED
An AVAST system in which an organism possesses a genome-encoded subtype IV locus represented by DefenseFinder with an Avs4A profile.
Trait evidence
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DOI:10.1126/science.aba0372AVAST, antiviral ATPase/NTPase of the STAND superfamily
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DOI:10.1126/science.abm4096Avs1 to Avs3 recognize the large terminase subunit, and Avs4 recognizes the portal
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DOI:10.1126/science.abm4096In all four cases, target recognition led to Avs protein activation and antiviral activity
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https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md| Avs | 10\.1126/science\.aba0372 | Diverse enzymatic activities mediate antiviral immunity in prokaryotes |
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https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md| Avs_IV__Avs4A | Avs_IV__Avs4A | Avs_IV | Custom | 60 |
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https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsvAvs Avs_IV 1 1 Avs_IV__Avs4A
Avs IV loci support phage portal recognition
NONMECHANISTIC · The graph captures Avs_IV at locus and Avs4 phage-portal recognition level without asserting the exact Avs4A component role, direct effector activity, native host breadth, sensitive-phage breadth, or whether every DefenseFinder Avs_IV prediction is a complete experimentally active Avs IV locus.
Edge evidence
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Avs IV locus
contributes to
Avs4 phage portal recognition
RO:0002326Avs IV loci encode Avs4 components, and Avs4 belongs to the AVAST receptors that recognize the phage portal protein.
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DOI:10.1126/science.abm4096Avs1 to Avs3 recognize the large terminase subunit, and Avs4 recognizes the portal -
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md| Avs_IV__Avs4A | Avs_IV__Avs4A | Avs_IV | Custom | 60 |
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Avs4 phage portal recognition
confers
Avs IV system
METPO:2007700The first-pass Avs IV system trait is realized by Avs4 target recognition and downstream antiviral activity.
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DOI:10.1126/science.abm4096Avs1 to Avs3 recognize the large terminase subunit, and Avs4 recognizes the portal -
DOI:10.1126/science.abm4096In all four cases, target recognition led to Avs protein activation and antiviral activity -
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsvAvs Avs_IV 1 1 Avs_IV__Avs4A
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Avs IV system
is a
AVAST system
rdfs:subClassOfAvs IV system possession is an AVAST-system trait.
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DOI:10.1126/science.aba0372AVAST, antiviral ATPase/NTPase of the STAND superfamily -
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md| Avs | 10\.1126/science\.aba0372 | Diverse enzymatic activities mediate antiviral immunity in prokaryotes | -
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsvAvs Avs_IV 1 1 Avs_IV__Avs4A
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Provenance
- Identifier source
- TraitMech local identifier
- Definition source
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv
Parent traits (1)
Synonyms (2)
- Avs_IV
- Avs_IV__Avs4A
kg-microbe context
No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.
Discussions and Knowledge Gaps
Resolve the Avs4A component role, direct effector chemistry, exact phage-trigger mapping, native host breadth, and sensitive-phage breadth before minting Avs IV mechanism or component children.
Gao et al. support Avs4 phage-portal recognition and Avs activation during antiviral defense, and the pinned DefenseFinder HMM inventory and rules table support Avs_IV as a subtype IV model with an Avs4A profile. This first-pass record leaves the exact component role, downstream effector chemistry, native host breadth, sensitive-phage breadth, and profile-to-activity requirements unresolved.
Evidence
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DOI:10.1126/science.abm4096Avs1 to Avs3 recognize the large terminase subunit, and Avs4 recognizes the portal
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DOI:10.1126/science.abm4096In all four cases, target recognition led to Avs protein activation and antiviral activity
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https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md| Avs_IV__Avs4A | Avs_IV__Avs4A | Avs_IV | Custom | 60 |
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https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsvAvs Avs_IV 1 1 Avs_IV__Avs4A
Curation history
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MINTED_TRAITMECH_ID · codex
Minted Avs IV system as a DOI- and DefenseFinder-backed GENOMICS TraitRecord under the AVAST 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_v414.
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REVIEW_CANONICAL_EXAMPLE_EVIDENCE_GAP · codex
Reviewed Avs IV system during initial curation and left canonical_examples empty because Gao et al. and the pinned DefenseFinder tables support the Avs_IV model namespace and Avs4 phage-portal-recognition activity but not an accession-backed native microbial taxon exemplar with experimentally verified endogenous Avs IV activity. No paid research was used.