{"metadata":{"accession":"F5BUE2","id":"F5BUE2_9MARC","source_organism":{"taxId":"989959","scientificName":"Kurzia trilobata","fullName":"Kurzia trilobata"},"name":"ATP synthase subunit beta","description":["Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits"],"length":380,"sequence":"GEPVDNLGPVDASTTFPIHRAAPAFTQLDTKLSIFETGIKVVDLSAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDINKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLRETIKGFQMILSGELDSLPEQAFYLVGNIDEATAKAATLQVEG","proteome":null,"gene":"atpB","go_terms":[{"identifier":"GO:0005524","name":"ATP binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0046933","name":"proton-transporting ATP synthase activity, rotational mechanism","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0015986","name":"proton motive force-driven ATP synthesis","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0045259","name":"proton-transporting ATP synthase complex","category":{"code":"C","name":"cellular_component"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":true,"in_alphafold":true,"in_bfvd":false,"ida_accession":"09b56d2b536f46f26a97332d3d29690e29f7828f","counters":{"domain_architectures":7029,"entries":20,"isoforms":0,"proteomes":0,"sets":3,"structures":0,"taxa":1,"dbEntries":{"cathgene3d":2,"cdd":2,"ssf":2,"pfam":2,"smart":1,"ncbifam":1,"panther":1,"prosite":1,"interpro":8},"proteome":0,"taxonomy":1,"similar_proteins":7029}}}