{"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}}