{"metadata":{"accession":"PF01934","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR008201","hierarchy":null,"name":{"name":"Ribonuclease HepT-like","short":"HepT-like"},"description":[{"text":"<p>This family includes the toxic component HepT of a type II toxin-antitoxin (TA) system, which has RNase activity. These proteins contain a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain and are neutralised through tri-AMPylation by the cognate antitoxin MntA, containing a MNT (minimal nucleotidyltransferase) domain [[cite:PUB00097221],[cite:PUB00097219],[cite:PUB00097220]]. HepT-MnA form an heterooctamer (at a 2:6 ratio), a rare organisation for this kind of TA systems. HepT dimerises and enables the formation of a deep cleft at the HEPN-domain interface, containing the RX4-6H motif (where X is any amino acid and the residue immediately after the conserved R is typically a polar amino acid) as the active site that functions as an RNA-cleaving RNase. This type II TA system regulates cell motility and confers plasmid stability [[cite:PUB00097219]]. Due to the prevalence of these HEPN/MNT modules in bacteria and archaea, it has been suggested that these TA systems may also play a role in the environmental adaptation to extreme habitats [[cite:PUB00097220]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00097219":{"PMID":29555683,"ISBN":null,"volume":"293","issue":"18","year":2018,"title":"Structure-function analyses reveal the molecular architecture and neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin system.","URL":null,"raw_pages":"6812-6823","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Jia X","Yao J","Gao Z","Liu G","Dong YH","Wang X","Zhang H."],"DOI_URL":null},"PUB00097221":{"PMID":26112399,"ISBN":null,"volume":"8","issue":"6","year":2015,"title":"Identification and characterization of a HEPN-MNT family type II toxin-antitoxin in Shewanella oneidensis.","URL":null,"raw_pages":"961-73","medline_journal":"Microb Biotechnol","ISO_journal":"Microb Biotechnol","authors":["Yao J","Guo Y","Zeng Z","Liu X","Shi F","Wang X."],"DOI_URL":null},"PUB00097220":{"PMID":33045733,"ISBN":null,"volume":"48","issue":"19","year":2020,"title":"Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system.","URL":null,"raw_pages":"11054-11067","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["Yao J","Zhen X","Tang K","Liu T","Xu X","Chen Z","Guo Y","Liu X","Wood TK","Ouyang S","Wang X."],"DOI_URL":null}},"set_info":{"accession":"CL0291","name":"KNTase_C"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":17,"interactions":0,"matches":7950,"pathways":0,"proteins":7949,"proteomes":4926,"sets":1,"structural_models":{"alphafold":5432},"structures":11,"taxa":8359},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":140,"alignment:full":4389},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7ae6","name":"Crystal structure of di-AMPylated HEPN(R102A) toxin"}}}