InterPro : IPR000477

Name  Reverse transcriptase domain Short Name  RT_dom
Type  Domain Description  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) (). Reverse transcriptase occurs in a variety of mobile elements, including retrotransposons, retroviruses, group II introns [], bacterial msDNAs, hepadnaviruses, and caulimoviruses.Retroviral 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 [].Several crystal structures of the reverse transcriptase (RT) domain have been determined [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR003545 Telomerase reverse transcriptase Telomerase_RT Family
IPR003286 RNA-directed DNA polymerase, eukaryota RNA_directed_DNA_poly_euk Family
IPR000123 RNA-directed DNA polymerase (reverse transcriptase), msDNA Reverse_transcriptase_msDNA Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Inouye S Structure, function, and evolution of bacterial reverse transcriptase. 1995 Virus Genes 11 81-94
Kohlstaedt LA Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. 1992 Science 256 1783-90
Schäfer B Reverse transcriptase and reverse splicing activities encoded by the mobile group II intron cobI1 of fission yeast mitochondrial DNA. 2003 J Mol Biol 329 191-206

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)