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Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "R9QS51",
"id": "R9QS51_EDWTA",
"source_organism": {
"taxId": "667121",
"scientificName": "Edwardsiella tarda ATCC 15947 = NBRC 105688",
"fullName": "Edwardsiella tarda ATCC 15947 = NBRC 105688"
},
"name": "60 kDa chaperonin",
"description": [
"Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding"
],
"length": 179,
"sequence": "AVAKAGKPLLIIAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGMELEKATLEDLGQAKRIVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGV",
"proteome": null,
"gene": "groEL",
"go_terms": [
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0140662",
"name": "ATP-dependent protein folding chaperone",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0042026",
"name": "protein refolding",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0006457",
"name": "protein folding",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"protein_evidence": 3,
"source_database": "unreviewed",
"is_fragment": true,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "bef8793fffa344cae7b4310cccda4040a454c532",
"counters": {
"domain_architectures": 111908,
"entries": 12,
"isoforms": 0,
"proteomes": 0,
"sets": 0,
"structures": 0,
"taxa": 1,
"dbEntries": {
"cathgene3d": 2,
"ssf": 1,
"pfam": 1,
"panther": 1,
"prints": 1,
"prosite": 1,
"interpro": 5
},
"proteome": 0,
"taxonomy": 1,
"similar_proteins": 111908
}
}
}