"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"IPR001313"	"{'subfamilies': 0, 'domain_architectures': 551, 'interactions': 1, 'matches': 194208, 'pathways': 4, 'proteins': 34346, 'proteomes': 3602, 'sets': 0, 'structural_models': {'alphafold': 29405, 'bfvd': 0}, 'structures': 78, 'taxa': 10282}"	"{'prositedoc': {'displayName': 'PROSITE Doc', 'description': 'PROSITE is a database of protein families and domains.', 'rank': 18, 'accessions': [{'accession': 'PDOC50302', 'url': 'http://prosite.expasy.org/PDOC50302'}]}}"	"[{'text': ""<p>Members of the Pumilio family of proteins (Puf) regulate translation and mRNA stability in a wide variety of eukaryotic organisms including mammals, flies, worms, slime mold, and yeast [[cite:PUB00018238]]. Pumilio family members are characterised by the presence of eight tandem copies of an imperfectly repeated 36 amino acids sequence motif, the Pumilio repeat, surrounded by a short N- and C-terminal conserved region. The eight repeats and the N- and C-terminal regions form the Pumilio homology domain (PUM-HD). The PUM-HD domain is a sequence-specific RNA binding domain. The Puf family of proteins are mainly post-transcriptional regulators. Several Puf members have been shown to bind specific RNA sequences mainly found in the 3' UTR of mRNA and repress their translation [[cite:PUB00018239], [cite:PUB00094378]]. Frequently, Puf proteins function asymmetrically to create protein gradients, thus causing asymmetric cell division and regulating cell fate specification [[cite:PUB00018240]].</p>\n\n<p>Crystal structure of Pumilio repeats has been solved [[cite:PUB00018241]]. The PUM repeat with the N- and C-terminal regions pack together to form a right-handed superhelix that approximates a half doughnut structurally similar to the Armadillo (ARM) repeat proteins, beta-catenin and\nkaryopherin alpha. The RNA binds the concave surface of the molecule, where\neach of the protein's eight repeats makes contacts with a different RNA base\nvia three amino acid side chains at conserved positions [[cite:PUB00018242]].</p>\n\n<p>This entry represents the Pumilio repeat.</p>"", 'llm': False, 'checked': False, 'updated': False}]"	""	"[{'identifier': 'GO:0003723', 'name': 'RNA binding', 'category': {'code': 'F', 'name': 'molecular_function'}}]"	"{'accession': 'IPR001313', 'name': 'Pumilio RNA-binding repeat', 'type': 'Repeat', 'children': []}"	""	False	False	False	"{'PUB00018238': {'PMID': 10662662, 'ISBN': None, 'volume': '10', 'issue': '2', 'year': 2000, 'title': 'Translational repression: a duet of Nanos and Pumilio.', 'URL': None, 'raw_pages': 'R81-3', 'medline_journal': 'Curr Biol', 'ISO_journal': 'Curr. Biol.', 'authors': ['Parisi M', 'Lin H.'], 'DOI_URL': 'http://dx.doi.org/10.1016/S0960-9822(00)00283-9'}, 'PUB00018239': {'PMID': 14584586, 'ISBN': None, 'volume': '55', 'issue': '7', 'year': 2003, 'title': 'The PUF family of RNA-binding proteins: does evolutionarily conserved structure equal conserved function?', 'URL': None, 'raw_pages': '359-66', 'medline_journal': 'IUBMB Life', 'ISO_journal': 'IUBMB Life', 'authors': ['Spassov DS', 'Jurecic R.'], 'DOI_URL': 'http://dx.doi.org/10.1080/15216540310001603093'}, 'PUB00018242': {'PMID': 12202039, 'ISBN': None, 'volume': '110', 'issue': '4', 'year': 2002, 'title': 'Modular recognition of RNA by a human pumilio-homology domain.', 'URL': None, 'raw_pages': '501-12', 'medline_journal': 'Cell', 'ISO_journal': 'Cell', 'authors': ['Wang X', 'McLachlan J', 'Zamore PD', 'Hall TM.'], 'DOI_URL': 'http://dx.doi.org/10.1016/S0092-8674(02)00873-5'}, 'PUB00018240': {'PMID': 1459455, 'ISBN': None, 'volume': '6', 'issue': '12A', 'year': 1992, 'title': 'Pumilio is essential for function but not for distribution of the Drosophila abdominal determinant Nanos.', 'URL': None, 'raw_pages': '2312-26', 'medline_journal': 'Genes Dev', 'ISO_journal': 'Genes Dev.', 'authors': ['Barker DD', 'Wang C', 'Moore J', 'Dickinson LK', 'Lehmann R.'], 'DOI_URL': 'http://www.genesdev.org/cgi/content/abstract/6/12A/2312'}, 'PUB00018241': {'PMID': 11336708, 'ISBN': None, 'volume': '7', 'issue': '4', 'year': 2001, 'title': 'Crystal structure of a Pumilio homology domain.', 'URL': None, 'raw_pages': '855-65', 'medline_journal': 'Mol Cell', 'ISO_journal': 'Mol. Cell', 'authors': ['Wang X', 'Zamore PD', 'Hall TM.'], 'DOI_URL': 'http://dx.doi.org/10.1016/S1097-2765(01)00229-5'}, 'PUB00094378': {'PMID': 29385744, 'ISBN': None, 'volume': '19', 'issue': '2', 'year': 2018, 'title': 'The PUF Protein Family: Overview on PUF RNA Targets, Biological Functions, and Post Transcriptional Regulation.', 'URL': None, 'raw_pages': None, 'medline_journal': 'Int J Mol Sci', 'ISO_journal': 'Int J Mol Sci', 'authors': ['Wang M', 'Oge L', 'Perez-Garcia MD', 'Hamama L', 'Sakr S.'], 'DOI_URL': None}, 'PUB00050752': {'PMID': 18328718, 'ISBN': None, 'volume': '16', 'issue': '4', 'year': 2008, 'title': 'Structures of human Pumilio with noncognate RNAs reveal molecular mechanisms for binding promiscuity.', 'URL': None, 'raw_pages': '549-57', 'medline_journal': 'Structure', 'ISO_journal': 'Structure', 'authors': ['Gupta YK', 'Nair DT', 'Wharton RP', 'Aggarwal AK.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.str.2008.01.006'}, 'PUB00050806': {'PMID': 18327269, 'ISBN': None, 'volume': '15', 'issue': '4', 'year': 2008, 'title': 'Basis of altered RNA-binding specificity by PUF proteins revealed by crystal structures of yeast Puf4p.', 'URL': None, 'raw_pages': '397-402', 'medline_journal': 'Nat Struct Mol Biol', 'ISO_journal': 'Nat. Struct. Mol. Biol.', 'authors': ['Miller MT', 'Higgin JJ', 'Hall TM.'], 'DOI_URL': 'http://dx.doi.org/10.1038/nsmb.1390'}, 'PUB00052211': {'PMID': 19540345, 'ISBN': None, 'volume': None, 'issue': None, 'year': 2009, 'title': 'Structure and RNA binding of the mouse Pumilio-2 Puf Domain.', 'URL': None, 'raw_pages': None, 'medline_journal': 'J Struct Biol', 'ISO_journal': 'J. Struct. Biol.', 'authors': ['Jenkins HT', 'Baker-Wilding R', 'Edwards TA.'], 'DOI_URL': None}, 'PUB00057141': {'PMID': 21653694, 'ISBN': None, 'volume': '286', 'issue': '30', 'year': 2011, 'title': 'Specific and modular binding code for cytosine recognition in Pumilio/FBF (PUF) RNA-binding domains.', 'URL': None, 'raw_pages': '26732-42', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Dong S', 'Wang Y', 'Cassidy-Amstutz C', 'Lu G', 'Bigler R', 'Jezyk MR', 'Li C', 'Hall TM', 'Wang Z.'], 'DOI_URL': 'http://dx.doi.org/10.1074/jbc.M111.244889'}}"	"{'pfam': {'PF22493': 'NOP9-like PUF repeat domain', 'PF00806': 'Pumilio-family RNA binding repeat'}, 'profile': {'PS50302': 'Pumilio RNA-binding repeat profile'}, 'smart': {'SM00025': 'Pumilio-like repeats'}}"	"{'name': 'Pumilio RNA-binding repeat', 'short': 'Pumilio_RNA-bd_rpt'}"	"[{'accession': 'IPR011989', 'name': 'Armadillo-like helical', 'type': 'homologous_superfamily'}, {'accession': 'IPR016024', 'name': 'Armadillo-type fold', 'type': 'homologous_superfamily'}]"	"{'accession': '5kla', 'name': 'Crystal structure of the drosophila Pumilio RNA-binding domain in complex with hunchback RNA'}"	""	"interpro"	"repeat"	""