{"metadata":{"accession":"P00798","id":"PEPA1_PENJA","source_organism":{"taxId":"5079","scientificName":"Penicillium janthinellum","fullName":"Penicillium janthinellum"},"name":"Penicillopepsin-1","description":["Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'"],"length":323,"sequence":"AASGVATNTPTANDEEYITPVTIGGTTLNLNFDTGSADLWVFSTELPASQQSGHSVYNPSATGKELSGYTWSISYGDGSSASGNVFTDSVTVGGVTAHGQAVQAAQQISAQFQQDTNNDGLLGLAFSSINTVQPQSQTTFFDTVKSSLAQPLFAVALKHQQPGVYDFGFIDSSKYTGSLTYTGVDNSQGFWSFNVDSYTAGSQSGDGFSGIADTGTTLLLLDDSVVSQYYSQVSGAQQDSNAGGYVFDCSTNLPDFSVSISGYTATVPGSLINYGPSGDGSTCLGGIQSNSGIGFSIFGDIFLKSQYVVFDSDGPQLGFAPQA","proteome":null,"gene":null,"go_terms":[{"identifier":"GO:0004190","name":"aspartic-type endopeptidase activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006508","name":"proteolysis","category":{"code":"P","name":"biological_process"}}],"protein_evidence":1,"source_database":"reviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"4f7e38ba910b0f25f406cea3df5f8e462e02113f","counters":{"domain_architectures":46498,"entries":13,"isoforms":0,"proteomes":0,"sets":2,"structures":14,"taxa":1,"dbEntries":{"cathgene3d":1,"ssf":1,"pfam":1,"profile":1,"cdd":1,"panther":1,"prosite":1,"prints":1,"interpro":5},"proteome":0,"taxonomy":1,"similar_proteins":46498}}}