{"metadata":{"accession":"PF09418","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR057668","hierarchy":null,"name":{"name":"Non-canonical E2 ubiquitin-conjugating enzyme, DUF2009 family","short":"DUF2009"},"description":[{"text":"<p>This entry represents a novel family of non-canonical E2 ubiquitin-conjugating enzymes that lack the typical HPN motif found in other E2 enzymes. The domain contains a highly conserved catalytic cysteine (C572 in PF3D7_0811400) that forms a thioester bond with ubiquitin. This was experimentally validated through mutational analysis and biochemical assays [[cite:PUB00160741]]. The domain is found in the C-terminal region of proteins, while the N-terminal region contains coiled helices involved in protein-protein interactions with other ubiquitin pathway components like Rbx1. The domain represents a new class of E2 enzymes particularly found in Apicomplexan parasites.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00160741":{"PMID":40249735,"ISBN":null,"volume":"21","issue":"4","year":2025,"title":"Activity-based protein profiling reveals both canonical and novel ubiquitin pathway enzymes in Plasmodium.","URL":null,"raw_pages":"e1013032","medline_journal":"PLoS Pathog","ISO_journal":"PLoS Pathog","authors":["Smith C","Hajisadeghian M","van Noort GJVH","Deery MJ","Pinto-Fernandez A","Kessler BM","Artavanis-Tsakonas K."],"DOI_URL":"https://doi.org/10.1371/journal.ppat.1013032"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":37,"interactions":0,"matches":1077,"pathways":0,"proteins":924,"proteomes":659,"sets":0,"structural_models":{"alphafold":769},"structures":0,"taxa":1643},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":40,"alignment:full":904},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}