{"metadata":{"accession":"PF01877","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002739","hierarchy":null,"name":{"name":"RNA binding","short":"RNA_binding"},"description":[{"text":"<p>PH1010 [swissprot:O58738] is composed of five alpha-helices (1-5) and eight beta-strands (1-8) with the following topology: beta-1, alpha-1, beta-2, beta-3, alpha-2, alpha-3, beta-4, beta-5, alpha-4, beta-6, alpha-5, beta-7, beta-8. The first six beta-strands (1-6) form a slightly twisted antiparallel beta-sheet and face five alpha-helices on one side. The last two beta-strands form an antiparallel beta-sheet in the C-terminus. PH1010 forms a characteristic homodimer structure in the crystal.                 Dimerisation of the molecule is crucial for function. The structure resembles that of some ribosomal proteins such as the 50S ribosomal protein L5 [[cite:PUB00051274]]. Although the structure resembles that of the RRM-type RNA-binding domain of the ribosomal L5 protein, the residues involved in RNA-binding in the L5 protein are not conserved in this family [[cite:PUB00048377]]. Despite this, these proteins bind to double-stranded RNA in a non-sequence specific manner [[cite:PUB00066786]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00066786":{"PMID":20380716,"ISBN":null,"volume":"3","issue":null,"year":2010,"title":"Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135.","URL":null,"raw_pages":"97","medline_journal":"BMC Res Notes","ISO_journal":"BMC Res Notes","authors":["Luz JS","Barbosa JA","Ramos CR","Oliveira CC."],"DOI_URL":"http://dx.doi.org/10.1186/1756-0500-3-97"},"PUB00048377":{"PMID":19079550,"ISBN":null,"volume":"3","issue":"12","year":2008,"title":"UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function.","URL":null,"raw_pages":"e3903","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Rao KN","Burley SK","Swaminathan S."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0003903"},"PUB00051274":{"PMID":18831045,"ISBN":null,"volume":"74","issue":"1","year":2009,"title":"Crystal structure of the DUF54 family protein PH1010 from hyperthermophilic archaea Pyrococcus horikoshii OT3.","URL":null,"raw_pages":"256-60","medline_journal":"Proteins","ISO_journal":"Proteins","authors":["Miyazono K","Shirokane M","Sawano Y","Tanokura M."],"DOI_URL":"http://dx.doi.org/10.1002/prot.22255"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":2,"interactions":0,"matches":1082,"pathways":0,"proteins":1082,"proteomes":562,"sets":0,"structural_models":{"alphafold":1034},"structures":7,"taxa":1009},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":80,"alignment:full":522},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2wny","name":"Structure of Mth689, a DUF54 protein from Methanothermobacter thermautotrophicus"}}}