{"metadata":{"accession":"PF13898","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR025257","hierarchy":null,"name":{"name":"Deubiquitinating enzyme MINDY-3/4, conserved domain","short":"MINDY-3_4_CD"},"description":[{"text":"<p>Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitination. This entry includes MINDY-3/4. They belong to the MINDY (motif interacting with Ub-containing novel DUB) family (peptidase family C121), whose members are deubiquitinating enzymes releasing Lys48-linked ubiquitin [[cite:PUB00081935]]. This is a conserved domain found in deubiquitinating enzymes, MINDY-3 and MINDY-4.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00081935":{"PMID":27292798,"ISBN":null,"volume":"63","issue":"1","year":2016,"title":"MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.","URL":null,"raw_pages":"146-55","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Abdul Rehman SA","Kristariyanto YA","Choi SY","Nkosi PJ","Weidlich S","Labib K","Hofmann K","Kulathu Y."],"DOI_URL":"http://dx.doi.org/10.1016/j.molcel.2016.05.009"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":66,"interactions":0,"matches":5272,"pathways":0,"proteins":4929,"proteomes":1768,"sets":0,"structural_models":{"alphafold":4295},"structures":0,"taxa":5489},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":31,"alignment:full":4095},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}