"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"
"IPR012108"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 1328, 'pathways': 0, 'proteins': 1328, 'proteomes': 696, 'sets': 0, 'structural_models': {'alphafold': 1250, 'bfvd': 0}, 'structures': 4, 'taxa': 2264}"	"{}"	"[{'text': '<p>This enzyme catalyzes the reverse reaction of mono-ADP-ribosylation by removing ADP-ribose from arginine residues in ADP-ribosylated proteins. NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyse opposing arms of the putative ADP-ribosylation cycle.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	"[{'identifier': 'GO:0000287', 'name': 'magnesium ion binding', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0003875', 'name': 'ADP-ribosylarginine hydrolase activity', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0051725', 'name': 'protein de-ADP-ribosylation', 'category': {'code': 'P', 'name': 'biological_process'}}]"	"{'accession': 'IPR005502', 'name': 'ADP-ribosylation/Crystallin J1', 'type': 'Family', 'children': [{'accession': 'IPR012108', 'name': 'ADP-ribosylarginine hydrolase', 'type': 'Family', 'children': []}, {'accession': 'IPR013479', 'name': 'ADP-ribosyl-dinitrogen reductase hydrolase', 'type': 'Family', 'children': []}, {'accession': 'IPR049650', 'name': 'ADP-ribosylarginine hydrolase Tri1-like', 'type': 'Family', 'children': []}]}"	""	False	False	False	"{'PUB00008412': {'PMID': 8349667, 'ISBN': None, 'volume': '268', 'issue': '24', 'year': 1993, 'title': 'Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase.', 'URL': None, 'raw_pages': '17837-43', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Takada T', 'Iida K', 'Moss J.'], 'DOI_URL': 'http://intl.jbc.org/cgi/content/abstract/268/24/17837'}, 'PUB00015992': {'PMID': 10358013, 'ISBN': None, 'volume': '274', 'issue': '24', 'year': 1999, 'title': 'Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases.', 'URL': None, 'raw_pages': '16736-40', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Konczalik P', 'Moss J.'], 'DOI_URL': 'http://dx.doi.org/10.1074/jbc.274.24.16736'}}"	"{'pirsf': {'PIRSF016939': 'ADP-ribosylarginine hydrolase'}}"	"{'name': 'ADP-ribosylarginine hydrolase', 'short': 'ADP-ribosylarg_hydro'}"	"[{'accession': 'IPR036705', 'name': 'ADP-ribosylation/Crystallin J1 superfamily', 'type': 'homologous_superfamily'}]"	"{'accession': '3hfw', 'name': 'Crystal Structure of human ADP-ribosylhydrolase 1 (hARH1)'}"	""	"interpro"	"family"	""