"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"
"PF02362"	"{'subfamilies': 0, 'domain_architectures': 769, 'interactions': 0, 'matches': 66564, 'pathways': 0, 'proteins': 50203, 'proteomes': 406, 'sets': 1, 'structural_models': {'alphafold': 43339, 'bfvd': 0}, 'structures': 21, 'taxa': 1472}"	"{}"	"[{'text': '<p>This is a family of plant transcription factors with various roles in development, the aligned region corresponds the B3 DNA binding domain as described in [[cite:PUB00008122]] this domain is found in VP1/AB13 transcription factors [[cite:PUB00019193]].  Some proteins also have a second AP2 DNA binding domain [pfam:PF00847] such as RAV1 [swissprot:Q9ZWM9] [[cite:PUB00008122]]. DNA binding activity was demonstrated by [[cite:PUB00018332]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR003340"	False	False	False	"{'PUB00019193': {'PMID': 9188533, 'ISBN': None, 'volume': '276', 'issue': '5320', 'year': 1997, 'title': 'ARF1, a transcription factor that binds to auxin response elements.', 'URL': None, 'raw_pages': '1865-8', 'medline_journal': 'Science', 'ISO_journal': 'Science', 'authors': ['Ulmasov T', 'Hagen G', 'Guilfoyle TJ.'], 'DOI_URL': 'http://dx.doi.org/10.1126/science.276.5320.1865'}, 'PUB00008122': {'PMID': 9862967, 'ISBN': None, 'volume': '27', 'issue': '2', 'year': 1999, 'title': 'RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants.', 'URL': None, 'raw_pages': '470-8', 'medline_journal': 'Nucleic Acids Res', 'ISO_journal': 'Nucleic Acids Res.', 'authors': ['Kagaya Y', 'Ohmiya K', 'Hattori T.'], 'DOI_URL': 'http://dx.doi.org/10.1093/nar/27.2.470'}, 'PUB00018332': {'PMID': 9165754, 'ISBN': None, 'volume': '9', 'issue': '5', 'year': 1997, 'title': 'The conserved B3 domain of VIVIPAROUS1 has a cooperative DNA binding activity.', 'URL': None, 'raw_pages': '799-807', 'medline_journal': 'Plant Cell', 'ISO_journal': 'Plant Cell', 'authors': ['Suzuki M', 'Kao CY', 'McCarty DR.'], 'DOI_URL': 'http://dx.doi.org/10.1105/tpc.9.5.799'}}"	""	"{'name': 'B3 DNA binding domain', 'short': 'B3'}"	""	"{'accession': '5os9', 'name': 'Structure of the B3 DNA-Binding Domain of NGA1'}"	"{'accession': 'CL0405', 'name': 'DNA_b-psBarrel'}"	"pfam"	"family"	"[{'title': 'B3_domain', 'extract': '<p>The B3 DNA binding domain (DBD) is a highly conserved domain found exclusively in transcription factors combined with other domains. It consists of 100-120 residues, includes seven beta strands and two alpha helices that form a DNA-binding pseudobarrel protein fold ; it interacts with the major groove of DNA.</p>', 'thumbnail': None}]"