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{
"metadata": {
"accession": "IPR037009",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": [
{
"identifier": "GO:0004651",
"name": "polynucleotide 5'-phosphatase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:3.20.100.10": "mRNA triphosphatase Cet1-like"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR037009",
"name": "mRNA triphosphatase Cet1-like superfamily",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "mRNA triphosphatase Cet1-like superfamily",
"short": "mRNA_triPase_Cet1_sf"
},
"description": [
{
"text": "<p>The mRNA capping enzyme in yeast is composed of two subunits, alpha and beta. The alpha subunit has guanylyltransferase activity, whilst the beta subunit is an RNA 5'-triphosphatase (RTPase) [[cite:PUB00044682]]. This entry represents a domain found in the mRNA capping enzyme beta subunit Cet1. RTPase catalyzes the first step in the mRNA cap formation process, the removal of the gamma-phosphate of triphosphate terminated pre-mRNA. This activity is metal-dependent. The 5'-end of the resulting mRNA diphosphate is subsequently capped with GMP by RNA guanylytransferase, and then further modified by one or more methyltransferases. The mRNA cap-forming activity is an essential step in mRNA processing. The RTPases are not conserved among eukarya and this subgroup includes fungal and protozoal RTPases. The RTPase domain of the mimivirus RTPase-GTase fusion mRNA capping enzyme also belongs to this subgroup. The domain is related to the CYTH domain. Cet1 has a novel active site fold whereby an eight-strand β-barrel forms a topologically closed tunnel known as the \"triphosphate tunnel\" [[cite:PUB00076463]]. Enzymes with similar structures are able to bind triphosphorylated substrates and requiring divalent metal ions as activators. They were thus called triphosphate tunnel metalloenzymes (TTMs) [[cite:PUB00076464], [cite:PUB00019882], [cite:PUB00024132], [cite:PUB00079677], [cite:PUB00079678], [cite:PUB00079679], [cite:PUB00079680], [cite:PUB00079681], [cite:PUB00079682], [cite:PUB00079683], [cite:PUB00010433], [cite:PUB00000015]].</p>\n\n<p>Cetl paralogue, Ctl1 (capping enzyme RNAtriphosphatase-like 1), is a RNA 5'-triphosphatase probably involved in an RNA processing event other than mRNA capping [[cite:PUB00075584]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000015": {
"PMID": 8418825,
"ISBN": null,
"volume": "27",
"issue": null,
"year": 1993,
"title": "Phylogeny of adenylyl cyclases.",
"URL": null,
"raw_pages": "109-62",
"medline_journal": "Adv Second Messenger Phosphoprotein Res",
"ISO_journal": "Adv. Second Messenger Phosphoprotein Res.",
"authors": [
"Danchin A."
],
"DOI_URL": null
},
"PUB00076464": {
"PMID": 24021036,
"ISBN": null,
"volume": "280",
"issue": "24",
"year": 2013,
"title": "Thiamine triphosphatase and the CYTH superfamily of proteins.",
"URL": null,
"raw_pages": "6443-55",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J.",
"authors": [
"Bettendorff L",
"Wins P."
],
"DOI_URL": "http://dx.doi.org/10.1111/febs.12498"
},
"PUB00079677": {
"PMID": 12788946,
"ISBN": null,
"volume": "278",
"issue": "33",
"year": 2003,
"title": "Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases.",
"URL": null,
"raw_pages": "30487-96",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Hausmann S",
"Pei Y",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M303060200"
},
"PUB00079678": {
"PMID": 11279161,
"ISBN": null,
"volume": "276",
"issue": "20",
"year": 2001,
"title": "Structure-function analysis of the active site tunnel of yeast RNA triphosphatase.",
"URL": null,
"raw_pages": "17261-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bisaillon M",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M100980200"
},
"PUB00079679": {
"PMID": 11395522,
"ISBN": null,
"volume": "276",
"issue": "32",
"year": 2001,
"title": "Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo.",
"URL": null,
"raw_pages": "30514-20",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bisaillon M",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M104936200"
},
"PUB00079683": {
"PMID": 11051760,
"ISBN": null,
"volume": "66",
"issue": null,
"year": 2001,
"title": "Structure, mechanism, and evolution of the mRNA capping apparatus.",
"URL": null,
"raw_pages": "1-40",
"medline_journal": "Prog Nucleic Acid Res Mol Biol",
"ISO_journal": "Prog. Nucleic Acid Res. Mol. Biol.",
"authors": [
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0079-6603(00)66025-7"
},
"PUB00079680": {
"PMID": 11279098,
"ISBN": null,
"volume": "276",
"issue": "18",
"year": 2001,
"title": "Importance of homodimerization for the in vivo function of yeast RNA triphosphatase.",
"URL": null,
"raw_pages": "14996-5002",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Lehman K",
"Ho CK",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M100588200"
},
"PUB00079681": {
"PMID": 9710603,
"ISBN": null,
"volume": "18",
"issue": "9",
"year": 1998,
"title": "Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus.",
"URL": null,
"raw_pages": "5189-98",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol. Cell. Biol.",
"authors": [
"Ho CK",
"Schwer B",
"Shuman S."
],
"DOI_URL": null
},
"PUB00010433": {
"PMID": 12456267,
"ISBN": null,
"volume": "3",
"issue": "1",
"year": 2002,
"title": "The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates.",
"URL": null,
"raw_pages": "33",
"medline_journal": "BMC Genomics",
"ISO_journal": "BMC Genomics",
"authors": [
"Iyer LM",
"Aravind L."
],
"DOI_URL": "http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=12456267&action=stream&blobtype=pdf"
},
"PUB00079682": {
"PMID": 12762032,
"ISBN": null,
"volume": "66",
"issue": null,
"year": 2001,
"title": "The mRNA capping apparatus as drug target and guide to eukaryotic phylogeny.",
"URL": null,
"raw_pages": "301-12",
"medline_journal": "Cold Spring Harb Symp Quant Biol",
"ISO_journal": "Cold Spring Harb. Symp. Quant. Biol.",
"authors": [
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1101/sqb.2001.66.301"
},
"PUB00044682": {
"PMID": 9345280,
"ISBN": null,
"volume": "239",
"issue": "1",
"year": 1997,
"title": "Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5'-triphosphatase, which is essential for cell viability.",
"URL": null,
"raw_pages": "116-22",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem. Biophys. Res. Commun.",
"authors": [
"Tsukamoto T",
"Shibagaki Y",
"Imajoh-Ohmi S",
"Murakoshi T",
"Suzuki M",
"Nakamura A",
"Gotoh H",
"Mizumoto K."
],
"DOI_URL": "http://dx.doi.org/10.1006/bbrc.1997.7439"
},
"PUB00024132": {
"PMID": 10589681,
"ISBN": null,
"volume": "99",
"issue": "5",
"year": 1999,
"title": "Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus.",
"URL": null,
"raw_pages": "533-43",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Lima CD",
"Wang LK",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(00)81541-X"
},
"PUB00075584": {
"PMID": 10219091,
"ISBN": null,
"volume": "27",
"issue": "10",
"year": 1999,
"title": "A Saccharomyces cerevisiae RNA 5'-triphosphatase related to mRNA capping enzyme.",
"URL": null,
"raw_pages": "2181-8",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Rodriguez CR",
"Takagi T",
"Cho EJ",
"Buratowski S."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/27.10.2181"
},
"PUB00019882": {
"PMID": 9755857,
"ISBN": null,
"volume": "435",
"issue": "1",
"year": 1998,
"title": "Isolation and characterization of the Candida albicans gene for mRNA 5'-triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-guanylyltransferase activities is essential for the function of mRNA 5'-capping enzyme in vivo.",
"URL": null,
"raw_pages": "49-54",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Yamada-Okabe T",
"Mio T",
"Matsui M",
"Kashima Y",
"Arisawa M",
"Yamada-Okabe H."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(98)01037-0"
},
"PUB00076463": {
"PMID": 16809816,
"ISBN": null,
"volume": "12",
"issue": "8",
"year": 2006,
"title": "Structure-function analysis of Plasmodium RNA triphosphatase and description of a triphosphate tunnel metalloenzyme superfamily that includes Cet1-like RNA triphosphatases and CYTH proteins.",
"URL": null,
"raw_pages": "1468-74",
"medline_journal": "RNA",
"ISO_journal": "RNA",
"authors": [
"Gong C",
"Smith P",
"Shuman S."
],
"DOI_URL": "http://dx.doi.org/10.1261/rna.119806"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR033469",
"name": "CYTH-like domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR004206",
"name": "mRNA triphosphatase Cet1-like",
"type": "domain"
},
{
"accession": "IPR040343",
"name": "RNA 5'-triphosphatase Cet1/Ctl1",
"type": "family"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 2586,
"pathways": 1,
"proteins": 2525,
"proteomes": 1697,
"sets": 0,
"structural_models": {
"alphafold": 2155,
"bfvd": 18
},
"structures": 12,
"taxa": 4194
},
"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": "3.6.1.74",
"url": "https://enzyme.expasy.org/EC/3.6.1.74"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3bgy",
"name": "Triclinic structure of Mimivirus Capping Enzyme Triphosphatase at 1.65 A"
}
}
}
