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{
"metadata": {
"accession": "PS50878",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR000477",
"hierarchy": null,
"name": {
"name": "Reverse transcriptase (RT) catalytic domain profile",
"short": "RT_POL"
},
"description": [
{
"text": "<p>Retroviral reverse transcriptases (EC 2.7.7.49) (prototypical RTs) exhibit\nthree enzymatic activities: an RNA-dependent DNA polymerase, Ribonuclease H,\nand a DNA-dependent DNA polymerase. These are employed in copying the plus\nstrand RNA genome to produce a minus strand of DNA, removal of the RNA\ntemplate, and synthesis of the plus strand of DNA using the minus-strand DNA\nas a template, respectively [[cite:PUB00018343]]. Both polymerase activities are performed by\nthe RT domain whereas the ribonuclease activity is achieved by the RNase H\ndomain.\n\nSeveral crystal structures of the RT domain have been determined (see for\nexample {PDB:3HVT}) [[cite:PUB00012846]]. Structurally, the RT domain can be divided in four\nsubdomains. Its anatomical resemblance to a right hand has led to naming the\nsubdomains as fingers, palm, and thumb. The fourth subdomain lies between the\nrest of the RT and the RNase H domain leading it to be called the connection\nsubdomain. The palm domain contains the catalytic triad critical for\npolymerase activity, and its folded structure resembles that of the\ncorresponding catalytic domain in other DNA and RNA polymerases. The position\nof fingers and thumb defined a deep cleft, with polymerase active residues at\nits base.\n\nProteins known to contain an RT domain are listed below:\n\n - Retroviral reverse transcriptase.\n - Catalytic subunit of the telomerase.\n - Eukaryotic retrotransposons.\n - Escherichia coli retroelement retron, which is responsible for the\n synthesis of multicopy single-stranded DNA (msDNA).\n - Bacterial mobile group II intron, that can reverse splice into DNA target\n substrate.\n\nThe finger, thumb and connection subdomains are less conserved among all RT\ndomain subfamilies [[cite:PUB00018344]] and could not be identified by the profile method. The\nprofile we developed is thus directed against the catalytic region (palm\nsubdomain).</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00012846": {
"PMID": 1377403,
"ISBN": null,
"volume": "256",
"issue": "5065",
"year": 1992,
"title": "Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor.",
"URL": null,
"raw_pages": "1783-90",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Kohlstaedt LA",
"Wang J",
"Friedman JM",
"Rice PA",
"Steitz TA."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/256/5065/1783"
},
"PUB00018343": {
"PMID": 7526778,
"ISBN": null,
"volume": "63",
"issue": null,
"year": 1994,
"title": "The retroviral enzymes.",
"URL": null,
"raw_pages": "133-73",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"Katz RA",
"Skalka AM."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.bi.63.070194.001025"
},
"PUB00018344": {
"PMID": 9703504,
"ISBN": null,
"volume": "281",
"issue": "5379",
"year": 1998,
"title": "The roles of structural imperfections in InGaN-based blue light-emitting diodes and laser diodes ",
"URL": null,
"raw_pages": "955-61",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Nakamura S."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.281.5379.956"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 714437,
"pathways": 0,
"proteins": 712318,
"proteomes": 10693,
"sets": 0,
"structural_models": {
"alphafold": 216229,
"bfvd": 167
},
"structures": 635,
"taxa": 29007
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "8bgj",
"name": "Crystal structure of Reverse Transcriptase domain from Caloramator australicus CART-CAPP"
}
}
}
