{"metadata":{"accession":"PF07717","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR011709","hierarchy":null,"name":{"name":"Oligonucleotide/oligosaccharide-binding (OB)-fold","short":"OB_NTP_bind"},"description":[{"text":"<p>This family is found towards the C-terminus of the DEAD-box helicases ([pfam:PF00270]). In these helicases it is apparently always found in association with [pfam:PF04408]. There do seem to be a couple of instances where it occurs by itself - e.g. [swissprot:Q84VZ2]. The structure PDB:3i4u adopts an OB-fold. helicases ([pfam:PF00270]). In these helicases it is apparently always found in association with [pfam:PF04408]. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins [[cite:PUB00092307]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00092307":{"PMID":20512115,"ISBN":null,"volume":"29","issue":"13","year":2010,"title":"Prp43p contains a processive helicase structural architecture with a specific regulatory domain.","URL":null,"raw_pages":"2194-204","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Walbott H","Mouffok S","Capeyrou R","Lebaron S","Humbert O","van Tilbeurgh H","Henry Y","Leulliot N."],"DOI_URL":"https://doi.org/10.1038/emboj.2010.102"},"PUB00152242":{"PMID":20696886,"ISBN":null,"volume":"107","issue":"34","year":2010,"title":"Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells.","URL":null,"raw_pages":"15181-6","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Kim T","Pazhoor S","Bao M","Zhang Z","Hanabuchi S","Facchinetti V","Bover L","Plumas J","Chaperot L","Qin J","Liu YJ."],"DOI_URL":"https://doi.org/10.1073/pnas.1006539107"}},"set_info":{"accession":"CL0021","name":"OB"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1449,"interactions":0,"matches":55670,"pathways":0,"proteins":55636,"proteomes":11620,"sets":1,"structural_models":{"alphafold":34331},"structures":160,"taxa":19634},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":54,"alignment:full":39591},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}