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{
"metadata": {
"accession": "IPR049821",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd07433": "Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE1"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR004013",
"name": "PHP domain",
"type": "Domain",
"children": [
{
"accession": "IPR003141",
"name": "Polymerase/histidinol phosphatase, N-terminal",
"type": "Domain",
"children": []
},
{
"accession": "IPR047967",
"name": "PolX, PHP domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR049821",
"name": "DnaE1-like, PHP domain",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "DnaE1-like, PHP domain",
"short": "PolIIIA_DnaE1_PHP"
},
"description": [
{
"text": "<p>DNA polymerase III alpha subunits (PolIIIAs) that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, standalone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterised protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. PolIIIA core enzyme catalyses the reaction for polymerising both DNA strands. DnaE1 is the longest compared to DnaE2 and DnaE3. A unique motif was also identified in dnaE1 and dnaE3 genes [[cite:PUB00019430], [cite:PUB00080354], [cite:PUB00122305], [cite:PUB00122304], [cite:PUB00122302]].</p>\n\n<p>This entry represents the PHP domain of DnaE1 type of the DNA polymerase III alpha subunit.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00019430": {
"PMID": 9685491,
"ISBN": null,
"volume": "26",
"issue": "16",
"year": 1998,
"title": "Phosphoesterase domains associated with DNA polymerases of diverse origins.",
"URL": null,
"raw_pages": "3746-52",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Aravind L",
"Koonin EV."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/26.16.3746"
},
"PUB00080354": {
"PMID": 21675919,
"ISBN": null,
"volume": "80",
"issue": null,
"year": 2011,
"title": "DNA replicases from a bacterial perspective.",
"URL": null,
"raw_pages": "403-36",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"McHenry CS."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev-biochem-061208-091655"
},
"PUB00122302": {
"PMID": 21855395,
"ISBN": null,
"volume": "15",
"issue": "5",
"year": 2011,
"title": "Bacterial replicases and related polymerases.",
"URL": null,
"raw_pages": "587-94",
"medline_journal": "Curr Opin Chem Biol",
"ISO_journal": "Curr Opin Chem Biol",
"authors": [
"McHenry CS."
],
"DOI_URL": null
},
"PUB00122304": {
"PMID": 17531796,
"ISBN": null,
"volume": "4",
"issue": "4",
"year": 2006,
"title": "Comparative analysis of eubacterial DNA polymerase III alpha subunits.",
"URL": null,
"raw_pages": "203-11",
"medline_journal": "Genomics Proteomics Bioinformatics",
"ISO_journal": "Genomics Proteomics Bioinformatics",
"authors": [
"Zhao XQ",
"Hu JF",
"Yu J."
],
"DOI_URL": null
},
"PUB00122305": {
"PMID": 22230424,
"ISBN": null,
"volume": "7",
"issue": null,
"year": 2012,
"title": "On the molecular mechanism of GC content variation among eubacterial genomes.",
"URL": null,
"raw_pages": "2",
"medline_journal": "Biol Direct",
"ISO_journal": "Biol Direct",
"authors": [
"Wu H",
"Zhang Z",
"Hu S",
"Yu J."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR016195",
"name": "Polymerase/histidinol phosphatase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 9877,
"pathways": 0,
"proteins": 9877,
"proteomes": 6325,
"sets": 0,
"structural_models": {
"alphafold": 7627,
"bfvd": 0
},
"structures": 9,
"taxa": 9944
},
"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": "4gx8",
"name": "Crystal structure of a DNA polymerase III alpha-epsilon chimera"
}
}
}
