{"metadata":{"accession":"cd13838","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":"IPR021983","hierarchy":null,"name":{"name":"Ribonuclease-like Prp8 domain IV core","short":"RNase_H_like_Prp8_IV"},"description":[{"text":"<p>This family contains Prp8 domain IV, which adopts a RNase H like fold within its core structure but with little sequence similarity. Prp8, a spliceosome protein, interacts directly with the splice sites and branch regions of precursor-mRNAs and spliceosomal RNAs associated with catalysis of the two steps of splicing. Catalysis of RNA cleavage by RNase H-like proteins involves a two-metal mechanism in which adjacently-bound divalent magnesium ions promote hydrolysis by activation of a water nucleophile and stabilization of the transition-state. However, the Prp8 domain IV contains only one of the canonical metal-binding sites and the coordinating side chains are spatially conserved with respect to Mg2+-coordinating residues within the RNase H fold. [[cite:PUB00051743]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00051743":{"PMID":18836455,"ISBN":null,"volume":"15","issue":"11","year":2008,"title":"Structural elucidation of a PRP8 core domain from the heart of the spliceosome.","URL":null,"raw_pages":"1199-205","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat. Struct. Mol. Biol.","authors":["Ritchie DB","Schellenberg MJ","Gesner EM","Raithatha SA","Stuart DT","Macmillan AM."],"DOI_URL":"http://dx.doi.org/10.1038/nsmb.1505"}},"set_info":{"accession":"cl14782","name":"RNase_H_like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":4531,"pathways":0,"proteins":4530,"proteomes":3115,"sets":1,"structural_models":{"alphafold":257,"bfvd":0},"structures":518,"taxa":8785},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4jk8","name":"Open and closed forms of R1865A human PRP8 RNase H-like domain with bound Mg ion"}}}