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{
"metadata": {
"accession": "IPR007012",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:1990817",
"name": "poly(A) RNA polymerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF04928": "Poly(A) polymerase central domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR007012",
"name": "Poly(A) polymerase, central domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Poly(A) polymerase, central domain",
"short": "PolA_pol_cen_dom"
},
"description": [
{
"text": "<p>In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the enzyme at the heart of the polyadenylation machinery, is a template-independent RNA polymerase which specifically incorporates ATP at the 3' end of mRNA. The crystal structure of bovine poly(A) polymerase bound to an ATP analog at 2.5 A resolution has been determined [[cite:PUB00008708]]. The structure revealed expected and unexpected similarities to other proteins. As expected, the catalytic domain of poly(A) polymerase shares substantial structural homology with other nucleotidyl transferases such as DNA polymerase beta and kanamycin transferase.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00008708": {
"PMID": 10944102,
"ISBN": null,
"volume": "19",
"issue": "16",
"year": 2000,
"title": "Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP.",
"URL": null,
"raw_pages": "4193-203",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Martin G",
"Keller W",
"Doublie S."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/19.16.4193"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 231,
"interactions": 0,
"matches": 12389,
"pathways": 14,
"proteins": 12278,
"proteomes": 3538,
"sets": 0,
"structural_models": {
"alphafold": 10624,
"bfvd": 1
},
"structures": 12,
"taxa": 9740
},
"entry_annotations": {
"alignment:seed": 88,
"alignment:full": 7974
},
"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": "2.7.7.19",
"url": "https://enzyme.expasy.org/EC/2.7.7.19"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
