The use of an RNA template to produce DNA, for integration into the host genome and exploitation of a host cell, is a strategy employed in the replication of retroid elements, such as the retroviruses and bacterial retrons. The enzyme catalysing polymerisation is an RNA-directed DNA-polymerase, or reverse trancriptase (RT) ([ec:2.7.7.49]). Reverse transcriptase occurs in a variety of mobile elements, including retrotransposons, retroviruses, group II introns [[cite:PUB00070025]], bacterial msDNAs, hepadnaviruses, and caulimoviruses.
\n\nRetroviral reverse transcriptase is synthesised as part of the POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, RNase H and integrase. POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. The discovery of retroelements in the prokaryotes raises intriguing questions concerning their roles in bacteria and the origin and evolution of reverse transcriptases and whether the bacterial reverse transcriptases are older than eukaryotic reverse transcriptases [[cite:PUB00006358]].
","llm":false,"checked":false,"updated":false},{"text":"Several crystal structures of the reverse transcriptase (RT) domain have been determined [[cite:PUB00012846]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00006358":{"PMID":8828137,"ISBN":null,"volume":"11","issue":"2-3","year":1995,"title":"Structure, function, and evolution of bacterial reverse transcriptase.","URL":null,"raw_pages":"81-94","medline_journal":"Virus Genes","ISO_journal":"Virus Genes","authors":["Inouye S","Inouye M."],"DOI_URL":"http://dx.doi.org/10.1007/BF01728650"},"PUB00070025":{"PMID":12758069,"ISBN":null,"volume":"329","issue":"2","year":2003,"title":"Reverse transcriptase and reverse splicing activities encoded by the mobile group II intron cobI1 of fission yeast mitochondrial DNA.","URL":null,"raw_pages":"191-206","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Schafer B","Gan L","Perlman PS."],"DOI_URL":"http://dx.doi.org/10.1016/S0022-2836(03)00441-8"},"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"}},"set_info":null,"overlaps_with":[{"accession":"IPR043502","name":"DNA/RNA polymerase superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":16915,"interactions":6,"matches":353222,"pathways":20,"proteins":348980,"proteomes":11333,"sets":0,"structural_models":{"alphafold":216249},"structures":651,"taxa":23000},"entry_annotations":{"alignment:seed":67,"alignment:full":197745},"cross_references":{"prositedoc":{"displayName":"PROSITE Doc","description":"PROSITE is a database of protein families and domains.","rank":18,"accessions":[{"accession":"PDOC50878","url":"http://prosite.expasy.org/PDOC50878"}]},"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":"2.7.7.49","url":"https://enzyme.expasy.org/EC/2.7.7.49"},{"accession":"2.7.7.7","url":"https://enzyme.expasy.org/EC/2.7.7.7"},{"accession":"3.1.26","url":"https://enzyme.expasy.org/EC/3.1.26"}]}},"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"}}}