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Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "I3V6P1",
"id": "I3V6P1_ACILW",
"source_organism": {
"taxId": "28090",
"scientificName": "Acinetobacter lwoffii",
"fullName": "Acinetobacter lwoffii"
},
"name": "Co-chaperonin GroES",
"description": [
"Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel"
],
"length": 133,
"sequence": "MACRVRPVLLSAVWHSLRATAKIAGFFHVNQPFTEVAMSNIKPLHDRVVIKRMEEEKLSAGGIVIPDSATEKPIKGEVVAVGTGKVLDNGQVRAPQVKVGDKVLFGKYSGTEVKLDGVELLVVKEDDLFAILG",
"proteome": null,
"gene": "groES",
"go_terms": [
{
"identifier": "GO:0006457",
"name": "protein folding",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0044183",
"name": "protein folding chaperone",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"protein_evidence": 3,
"source_database": "unreviewed",
"is_fragment": false,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "96ac8ba8a540be879c6c062e6821e3878208f354",
"counters": {
"domain_architectures": 38603,
"entries": 17,
"isoforms": 0,
"proteomes": 0,
"sets": 2,
"structures": 0,
"taxa": 1,
"dbEntries": {
"cathgene3d": 1,
"ssf": 1,
"pfam": 1,
"smart": 1,
"cdd": 1,
"panther": 1,
"ncbifam": 4,
"hamap": 1,
"prosite": 1,
"prints": 1,
"interpro": 4
},
"proteome": 0,
"taxonomy": 1,
"similar_proteins": 38603
}
}
}