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{
"metadata": {
"accession": "PS51549",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR019545",
"hierarchy": null,
"name": {
"name": "DM13 domain profile",
"short": "DM13"
},
"description": [
{
"text": "<p>The DM13 domain has been identified in animal proteins containing a DOMON\ndomain likely to function as cytochromes involved in as yet\nunidentified redox reactions potentially related to protein hydroxylation or\noxidative cross-linking. However, it is also found in bacteria. The DM13\ndomain contains a nearly absolutely conserved cysteine, which can be\npotentially involved in a redox reaction either as a nacked thiol group or by\nbinding a prosthetic group like heme [[cite:PUB00044228]].\n\nThe DM13 domain is predicted to have a beta-strand-rich fold [[cite:PUB00044228]].\n\nThe profile we developed covers the entire DM13 domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00044228": {
"PMID": 17878204,
"ISBN": null,
"volume": "23",
"issue": "20",
"year": 2007,
"title": "The DOMON domains are involved in heme and sugar recognition.",
"URL": null,
"raw_pages": "2660-4",
"medline_journal": "Bioinformatics",
"ISO_journal": "Bioinformatics",
"authors": [
"Iyer LM",
"Anantharaman V",
"Aravind L."
],
"DOI_URL": "http://dx.doi.org/10.1093/bioinformatics/btm411"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 7621,
"pathways": 0,
"proteins": 6041,
"proteomes": 3065,
"sets": 0,
"structural_models": {
"alphafold": 4593,
"bfvd": 0
},
"structures": 0,
"taxa": 6991
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
