"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"
"IPR002379"	"{'subfamilies': 0, 'domain_architectures': 327, 'interactions': 0, 'matches': 81222, 'pathways': 67, 'proteins': 65500, 'proteomes': 21227, 'sets': 0, 'structural_models': {'alphafold': 56933, 'bfvd': 0}, 'structures': 426, 'taxa': 61948}"	"{'gp': {'displayName': 'Genome Properties', 'description': 'Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.', 'rank': 45, 'accessions': [{'accession': 'GenProp0128', 'url': 'https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0128'}]}}"	"[{'text': ""<p>The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis  [[cite:PUB00009752], [cite:PUB00020609]].</p>\r\n\r\n<p>In V-ATPases, there are three proteolipid subunits (c, c' and c'') that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, and together they form a hexameric ring spanning the membrane [[cite:PUB00020629], [cite:PUB00020631]].</p>"", 'llm': False, 'checked': False, 'updated': False}, {'text': '<p>Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	"[{'identifier': 'GO:0015078', 'name': 'proton transmembrane transporter activity', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:1902600', 'name': 'proton transmembrane transport', 'category': {'code': 'P', 'name': 'biological_process'}}, {'identifier': 'GO:0033177', 'name': 'proton-transporting two-sector ATPase complex, proton-transporting domain', 'category': {'code': 'C', 'name': 'cellular_component'}}]"	"{'accession': 'IPR002379', 'name': 'V-ATPase proteolipid subunit C-like domain', 'type': 'Domain', 'children': []}"	""	False	False	False	"{'PUB00068788': {'PMID': 1385979, 'ISBN': None, 'volume': '1101', 'issue': '2', 'year': 1992, 'title': 'F-type or V-type? The chimeric nature of the archaebacterial ATP synthase.', 'URL': None, 'raw_pages': '232-5', 'medline_journal': 'Biochim Biophys Acta', 'ISO_journal': 'Biochim. Biophys. Acta', 'authors': ['Schafer G', 'Meyering-Vos M.'], 'DOI_URL': None}, 'PUB00068789': {'PMID': 9741106, 'ISBN': None, 'volume': '21', 'issue': '1', 'year': 1998, 'title': 'F-and V-ATPases in the genus Thermus and related species.', 'URL': None, 'raw_pages': '12-22', 'medline_journal': 'Syst Appl Microbiol', 'ISO_journal': 'Syst. Appl. Microbiol.', 'authors': ['Radax C', 'Sigurdsson O', 'Hreggvidsson GO', 'Aichinger N', 'Gruber C', 'Kristjansson JK', 'Stan-Lotter H.'], 'DOI_URL': None}, 'PUB00068786': {'PMID': 20450191, 'ISBN': None, 'volume': '49', 'issue': '23', 'year': 2010, 'title': 'Regulation and isoform function of the V-ATPases.', 'URL': None, 'raw_pages': '4715-23', 'medline_journal': 'Biochemistry', 'ISO_journal': 'Biochemistry', 'authors': ['Toei M', 'Saum R', 'Forgac M.'], 'DOI_URL': 'http://dx.doi.org/10.1021/bi100397s'}, 'PUB00068787': {'PMID': 18937357, 'ISBN': None, 'volume': '30', 'issue': '11-12', 'year': 2008, 'title': 'New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0).', 'URL': None, 'raw_pages': '1096-109', 'medline_journal': 'Bioessays', 'ISO_journal': 'Bioessays', 'authors': ['Gruber G', 'Marshansky V.'], 'DOI_URL': 'http://dx.doi.org/10.1002/bies.20827'}, 'PUB00020629': {'PMID': 15951435, 'ISBN': None, 'volume': '280', 'issue': '30', 'year': 2005, 'title': 'Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain.', 'URL': None, 'raw_pages': '27896-903', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Inoue T', 'Forgac M.'], 'DOI_URL': 'http://dx.doi.org/10.1074/jbc.M504890200'}, 'PUB00056210': {'PMID': 19783985, 'ISBN': None, 'volume': '16', 'issue': '10', 'year': 2009, 'title': 'High-resolution structure of the rotor ring of a proton-dependent ATP synthase.', 'URL': None, 'raw_pages': '1068-73', 'medline_journal': 'Nat Struct Mol Biol', 'ISO_journal': 'Nat. Struct. Mol. Biol.', 'authors': ['Pogoryelov D', 'Yildiz O', 'Faraldo-Gomez JD', 'Meier T.'], 'DOI_URL': 'http://dx.doi.org/10.1038/nsmb.1678'}, 'PUB00009752': {'PMID': 11309608, 'ISBN': None, 'volume': '410', 'issue': '6831', 'year': 2001, 'title': 'Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.', 'URL': None, 'raw_pages': '898-904', 'medline_journal': 'Nature', 'ISO_journal': 'Nature', 'authors': ['Yasuda R', 'Noji H', 'Yoshida M', 'Kinosita K Jr', 'Itoh H.'], 'DOI_URL': 'http://dx.doi.org/10.1038/35073513'}, 'PUB00020609': {'PMID': 15629643, 'ISBN': None, 'volume': '36', 'issue': '2', 'year': 2005, 'title': 'A structural model of the vacuolar ATPase from transmission electron microscopy.', 'URL': None, 'raw_pages': '109-26', 'medline_journal': 'Micron', 'ISO_journal': 'Micron', 'authors': ['Wilkens S', 'Zhang Z', 'Zheng Y.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.micron.2004.10.002'}, 'PUB00020604': {'PMID': 15078220, 'ISBN': None, 'volume': '5', 'issue': '2', 'year': 2004, 'title': 'Mechanisms of ATPases--a multi-disciplinary approach.', 'URL': None, 'raw_pages': '89-105', 'medline_journal': 'Curr Protein Pept Sci', 'ISO_journal': 'Curr. Protein Pept. Sci.', 'authors': ['Rappas M', 'Niwa H', 'Zhang X.'], 'DOI_URL': 'http://dx.doi.org/10.2174/1389203043486874'}, 'PUB00020603': {'PMID': 15473999, 'ISBN': None, 'volume': '576', 'issue': '1-2', 'year': 2004, 'title': 'The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.', 'URL': None, 'raw_pages': '1-4', 'medline_journal': 'FEBS Lett', 'ISO_journal': 'FEBS Lett.', 'authors': ['Cross RL', 'Muller V.'], 'DOI_URL': 'http://dx.doi.org/10.1016/j.febslet.2004.08.065'}, 'PUB00020631': {'PMID': 14635779, 'ISBN': None, 'volume': '35', 'issue': '4', 'year': 2003, 'title': 'Structure and function of the vacuolar H+-ATPase: moving from low-resolution models to high-resolution structures.', 'URL': None, 'raw_pages': '337-45', 'medline_journal': 'J Bioenerg Biomembr', 'ISO_journal': 'J. Bioenerg. Biomembr.', 'authors': ['Harrison M', 'Durose L', 'Song CF', 'Barratt E', 'Trinick J', 'Jones R', 'Findlay JB.'], 'DOI_URL': 'http://dx.doi.org/10.1023/A:1025728915565'}}"	"{'pfam': {'PF00137': 'ATP synthase subunit C'}}"	"{'name': 'V-ATPase proteolipid subunit C-like domain', 'short': 'ATPase_proteolipid_c-like_dom'}"	"[{'accession': 'IPR038662', 'name': 'F1F0 ATP synthase subunit C superfamily', 'type': 'homologous_superfamily'}, {'accession': 'IPR035921', 'name': 'F/V-ATP synthase subunit C superfamily', 'type': 'homologous_superfamily'}]"	"{'accession': '4f4s', 'name': 'Structure of the yeast F1Fo ATPase c10 ring with bound oligomycin'}"	""	"interpro"	"domain"	""