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InterPro: IPR000477 RNA-directed DNA polymerase (reverse transcriptase)

Protein matchesHelp
UniProtKB
Matches:
118616 proteins
AccessionHelp IPR000477 Reverse_transcriptase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR000123 RNA-directed DNA polymerase (reverse transcriptase), msDNA
IPR003286 Nematode reverse transcriptase-like
IPR003545 Telomere reverse transcriptase
IPR015706 RNA-directed DNA polymerase (reverse transcriptase), related
GO Term annotationHelp
Process GO:0006278 RNA-dependent DNA replication
Function GO:0003723 RNA binding
GO:0003964 RNA-directed DNA polymerase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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, 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 [1].

Structural linksHelp
PDB - click here
SCOP: e.8.1.2
Database linksHelp
Enzyme: EC:2.7.7.49
PROSITE doc: PDOC50878
PANDIT: PF00078
Pfam Clan: CL0024.14
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000477 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14746 Telomerase reverse transcriptase

O70372 Telomerase reverse transcriptase

P03875 Putative COX1/OXI3 intron 1 protein

P04323 Retrovirus-related Pol polyprotein from transposon 17.6

P34620 Putative uncharacterized transposon-derived protein ZK1236.4

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000442 Intron maturase, type II
IPR003615 HNH nuclease
IPR012337 Polynucleotidyl transferase, ribonuclease H fold
IPR000477 RNA-directed DNA polymerase (reverse transcriptase)
IPR003545 Telomere reverse transcriptase
IPR003286 Nematode reverse transcriptase-like
IPR015706 RNA-directed DNA polymerase (reverse transcriptase), related
IPR001584 Integrase, catalytic core
IPR018061 Peptidase A2A, retrovirus RVP subgroup
IPR000883 Cytochrome c oxidase, subunit I
IPR009007 Peptidase aspartic, catalytic
ModBase
SWISS-MODEL

PublicationsHelp
1. Inouye S, Inouye M.
Structure, function, and evolution of bacterial reverse transcriptase.
Virus Genes 11 81-94 1995 [PubMed: 8828137]
http://dx.doi.org/10.1007/BF01728650

Additional ReadingHelp
Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA.
Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor.
Science 256 1992 1783-90 [PubMed: 1377403]
http://www.sciencemag.org/cgi/content/abstract/256/5065/1783
Xiong Y, Eickbush TH.
Origin and evolution of retroelements based upon their reverse transcriptase sequences.
EMBO J. 9 1990 3353-62 [PubMed: 1698615]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1698615
Tucker TJ, Sisko JT, Tynebor RM, Williams TM, Felock PJ, Flynn JA, Lai MT, Liang Y, McGaughey G, Liu M, Miller M, Moyer G, Munshi V, Perlow-Poehnelt R, Prasad S, Reid JC, Sanchez R, Torrent M, Vacca JP, Wan BL, Yan Y.
Discovery of 3-{5-[(6-amino-1H-pyrazolo[3,4-b]pyridine-3-yl)methoxy]-2-chlorophenoxy}-5-chlorobenzonitrile (MK-4965): a potent, orally bioavailable HIV-1 non-nucleoside reverse transcriptase inhibitor with improved potency against key mutant viruses.
J. Med. Chem. 51 2008 6503-11 [PubMed: 18826204]
http://dx.doi.org/10.1021/jm800856c
Das K, Bauman JD, Clark AD Jr, Frenkel YV, Lewi PJ, Shatkin AJ, Hughes SH, Arnold E.
High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 1466-71 [PubMed: 18230722]
http://dx.doi.org/10.1073/pnas.0711209105
Venteicher AS, Meng Z, Mason PJ, Veenstra TD, Artandi SE.
Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly.
Cell 132 2008 945-57 [PubMed: 18358808]
http://dx.doi.org/10.1016/j.cell.2008.01.019
Spallarossa A, Cesarini S, Ranise A, Ponassi M, Unge T, Bolognesi M.
Crystal structures of HIV-1 reverse transcriptase complexes with thiocarbamate non-nucleoside inhibitors.
Biochem. Biophys. Res. Commun. 365 2008 764-70 [PubMed: 18035053]
http://dx.doi.org/10.1016/j.bbrc.2007.11.036
Goodwin KD, Lewis MA, Long EC, Georgiadis MM.
Crystal structure of DNA-bound Co(III) bleomycin B2: Insights on intercalation and minor groove binding.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 5052-6 [PubMed: 18362349]
http://dx.doi.org/10.1073/pnas.0708143105
Katz RA, Skalka AM.
The retroviral enzymes.
Annu. Rev. Biochem. 63 1994 133-73 [PubMed: 7526778]
http://dx.doi.org/10.1146/annurev.bi.63.070194.001025
Bauman JD, Das K, Ho WC, Baweja M, Himmel DM, Clark AD Jr, Oren DA, Boyer PL, Hughes SH, Shatkin AJ, Arnold E.
Crystal engineering of HIV-1 reverse transcriptase for structure-based drug design.
Nucleic Acids Res. 36 2008 5083-92 [PubMed: 18676450]
http://dx.doi.org/10.1093/nar/gkn464
Nakamura S.
The roles of structural imperfections in InGaN-based blue light-emitting diodes and laser diodes
Science 281 1998 955-61 [PubMed: 9703504]
http://dx.doi.org/10.1126/science.281.5379.956
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InterPro 23.1