HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "IPR018320",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0003887",
"name": "DNA-directed DNA polymerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006260",
"name": "DNA replication",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR00593": "DNA polymerase I"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR002298",
"name": "DNA polymerase A",
"type": "Family",
"children": [
{
"accession": "IPR018320",
"name": "DNA polymerase 1",
"type": "Family",
"children": []
},
{
"accession": "IPR034699",
"name": "DNA-directed DNA polymerase T7",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "DNA polymerase 1",
"short": "DNA_polymerase_1"
},
"description": [
{
"text": "<p>DNA carries the biological information that instructs cells how to exist in an ordered fashion. Accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA polymerases, which add nucleotide triphosphate (dNTP) residues to the 3'-end of the growing DNA chain, using a complementary DNA as template. Small RNA molecules are generally used as primers for chain elongation, although terminal proteins may also be used. DNA-dependent DNA polymerases have been grouped into families, denoted A, B and X, on the basis of sequence similarities [[cite:PUB00004647], [cite:PUB00004955]]. Members of family A, which includes bacterial and bacteriophage polymerases, share significant similarity to Escherichia coli polymerase I; hence family A is also known as the pol I family. The bacterial polymerases also contain an exonuclease activity, which is coded for in the N-terminal portion. Three motifs, A, B and C [[cite:PUB00004955]], are seen to be conserved across all DNA polymerases, with motifs A and C also seen in RNA polymerases. They are centred on invariant residues, and their structural significance was implied from the Klenow (E. coli) structure. Motif A contains a strictly-conserved aspartate at the junction of a β-strand and an α-helix; motif B contains an α-helix with positive charges; and motif C has a doublet of negative charges, located in a β-turn-beta secondary structure [[cite:PUB00004955]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004647": {
"PMID": 3479792,
"ISBN": null,
"volume": "84",
"issue": "23",
"year": 1987,
"title": "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.",
"URL": null,
"raw_pages": "8287-91",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Jung GH",
"Leavitt MC",
"Hsieh JC",
"Ito J."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=3479792&action=stream&blobtype=pdf"
},
"PUB00004955": {
"PMID": 2196557,
"ISBN": null,
"volume": "3",
"issue": "6",
"year": 1990,
"title": "An attempt to unify the structure of polymerases.",
"URL": null,
"raw_pages": "461-7",
"medline_journal": "Protein Eng",
"ISO_journal": "Protein Eng.",
"authors": [
"Delarue M",
"Poch O",
"Tordo N",
"Moras D",
"Argos P."
],
"DOI_URL": "http://dx.doi.org/10.1093/protein/3.6.461"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 25797,
"pathways": 0,
"proteins": 25797,
"proteomes": 16747,
"sets": 0,
"structural_models": {
"alphafold": 19790,
"bfvd": 0
},
"structures": 230,
"taxa": 27297
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.7.7.7",
"url": "https://enzyme.expasy.org/EC/2.7.7.7"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3pv8",
"name": "Crystal Structure of Bacillus DNA Polymerase I Large Fragment Bound to DNA and ddTTP-dA in Closed Conformation"
}
}
}
