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{
"metadata": {
"accession": "IPR007434",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR47017": "ACYL-COA"
},
"pfam": {
"PF04339": "Peptidogalycan biosysnthesis/recognition"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR007434",
"name": "Peptidogalycan biosysnthesis/recognition",
"type": "Family",
"children": []
},
"name": {
"name": "Peptidogalycan biosysnthesis/recognition",
"short": "FemAB-like"
},
"description": [
{
"text": "<p>This is a family of both bacterial and plant proteins with responsibility for building interpeptide bridges in peptidoglycan. Such a function is feasible for bacteria but less likely for the plant members of this family. Perhaps the plant-members are using homologous proteins to recognise bacterial peptidoglcans as part of their innate immune system [[cite:PUB00075353]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00075353": {
"PMID": 20537955,
"ISBN": null,
"volume": "34",
"issue": "3",
"year": 2010,
"title": "The challenge of annotating protein sequences: The tale of eight domains of unknown function in Pfam.",
"URL": null,
"raw_pages": "210-4",
"medline_journal": "Comput Biol Chem",
"ISO_journal": "Comput Biol Chem",
"authors": [
"Goonesekere NC",
"Shipely K",
"O'Connor K."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.compbiolchem.2010.04.001"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 31,
"interactions": 0,
"matches": 9551,
"pathways": 0,
"proteins": 9453,
"proteomes": 6242,
"sets": 0,
"structural_models": {
"alphafold": 7055,
"bfvd": 0
},
"structures": 0,
"taxa": 10528
},
"entry_annotations": {
"alignment:seed": 50,
"alignment:full": 3791
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}