{"metadata":{"accession":"PF26994","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR059364","hierarchy":null,"name":{"name":"Domain of unknown function (DUF8320)","short":"DUF8320"},"description":[{"text":"<p>This entry represents a domain of unknown function at the N-terminal in uncharacterised proteins mostly found in bacteria. This domain belongs to proteins with a conserved four or five-helix up-and-down bundle structure. This structure is typical of focal adhesion targeting (FAT) domains and is responsible for dimerisation. These proteins are also present in transcriptional regulators where the bundle structure is important for their dynamic conformational equilibrium to control target specificity. The conserved helical bundle architecture enables these proteins to function in protein-protein interactions and regulatory processes [[cite:PUB00075415],[cite:PUB00004911],[cite:PUB00161916]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Domain_of_unknown_function","extract":"<p>A <b>domain of unknown function</b> (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.</p>","thumbnail":null}],"literature":{"PUB00075415":{"PMID":20399778,"ISBN":null,"volume":"584","issue":"11","year":2010,"title":"The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.","URL":null,"raw_pages":"2237-41","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["Goult BT","Gingras AR","Bate N","Barsukov IL","Critchley DR","Roberts GC."],"DOI_URL":"http://dx.doi.org/10.1016/j.febslet.2010.04.028"},"PUB00004911":{"PMID":9159132,"ISBN":null,"volume":"94","issue":"11","year":1997,"title":"The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals.","URL":null,"raw_pages":"5679-84","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["McCann RO","Craig SW."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.94.11.5679"},"PUB00161916":{"PMID":28860193,"ISBN":null,"volume":"292","issue":"44","year":2017,"title":"Structural and functional insights into the interaction between the Cas family scaffolding protein p130Cas and the focal adhesion-associated protein paxillin.","URL":null,"raw_pages":"18281-18289","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Zhang C","Miller DJ","Guibao CD","Donato DM","Hanks SK","Zheng JJ."],"DOI_URL":"https://doi.org/10.1074/jbc.M117.807271"}},"set_info":{"accession":"CL0705","name":"VBS-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":4,"interactions":0,"matches":706,"pathways":0,"proteins":706,"proteomes":491,"sets":1,"structural_models":{"alphafold":415},"structures":0,"taxa":637},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":115,"alignment:full":345},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}