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InterPro: IPR006592 RNA polymerase, N-terminal

Protein matchesHelp
UniProtKB
Matches:
5696 proteins
AccessionHelp IPR006592 RNA_pol_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR012754 DNA-directed RNA polymerase, subunit beta-prime
IPR012755 DNA-directed RNA polymerase, subunit gamma
IPR012758 DNA-directed RNA polymerase, subunit A'
IPR015699 DNA-directed RNA pol I, largest subunit
IPR015700 DNA-directed RNA polymerase III largest subunit
Contains IPR000722 RNA polymerase, alpha subunit
GO Term annotationHelp
Process GO:0006350 transcription
Function GO:0003677 DNA binding
GO:0003899 DNA-directed RNA polymerase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The task of transcribing nuclear genes is shared between three RNA polymerases in eukaryotes: RNA polymerase (pol) I synthesizes the large rRNA, pol II synthesizes mRNA and pol III synthesizes tRNA and 5S rRNA [1]. Pol I transcription is localised to discrete sites called nucleoli; these can be likened to ribosome factories, in which rRNA is synthesised by pol I in the fibrillar centres and then processed and assembled into ribosomes in the surrounding granular regions [2]. Prokaryotes, in contrast, posses a single RNA polymerase, with transcription being controlled by the particular signam factor interacting with the catalytic core.

This entry describes an N-terminal conserved region which can be found in the largest subunits of prokaryoptic and eukaryotic RNA polymerases.

Structural linksHelp
PDB - click here
SCOP: e.29.1.2 , i.8.1.1
Database linksHelp
Enzyme: EC:2.7.7.6
Blocks: IPB006592

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006592 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14802 DNA-directed RNA polymerase III subunit RPC1

O35134 DNA-directed RNA polymerase I subunit RPA1

P04050 DNA-directed RNA polymerase II subunit RPB1

P04052 DNA-directed RNA polymerase II subunit RPB1

P16356 DNA-directed RNA polymerase II subunit RPB1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR007083 RNA polymerase Rpb1, domain 4
IPR007080 RNA polymerase Rpb1, domain 1
IPR007081 RNA polymerase Rpb1, domain 5
IPR015699 DNA-directed RNA pol I, largest subunit
IPR006592 RNA polymerase, N-terminal
IPR000684 RNA polymerase II, heptapeptide repeat, eukaryotic
IPR000722 RNA polymerase, alpha subunit
IPR007066 RNA polymerase Rpb1, domain 3
IPR007075 RNA polymerase Rpb1, domain 6
IPR007073 RNA polymerase Rpb1, domain 7
PDB Chain
ModBase
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Paule MR, White RJ.
Survey and summary: transcription by RNA polymerases I and III.
Nucleic Acids Res. 28 1283-98 2000 [PubMed: 10684922]
http://dx.doi.org/10.1093/nar/28.6.1283
2. Shaw PJ, Jordan EG.
The nucleolus.
Annu. Rev. Cell Dev. Biol. 11 93-121 1995 [PubMed: 8689574]
http://dx.doi.org/10.1146/annurev.cb.11.110195.000521

Additional ReadingHelp
Vassylyev DG, Vassylyeva MN, Zhang J, Palangat M, Artsimovitch I, Landick R.
Structural basis for substrate loading in bacterial RNA polymerase.
Nature 448 2007 163-8 [PubMed: 17581591]
http://dx.doi.org/10.1038/nature05931
Brueckner F, Cramer P.
Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation.
Nat. Struct. Mol. Biol. 15 2008 811-8 [PubMed: 18552824]
http://dx.doi.org/10.1038/nsmb.1458
Kaplan CD, Larsson KM, Kornberg RD.
The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by alpha-amanitin.
Mol. Cell 30 2008 547-56 [PubMed: 18538653]
http://dx.doi.org/10.1016/j.molcel.2008.04.023
Brueckner F, Hennecke U, Carell T, Cramer P.
CPD damage recognition by transcribing RNA polymerase II.
Science 315 2007 859-62 [PubMed: 17290000]
http://dx.doi.org/10.1126/science.1135400
Mukhopadhyay J, Das K, Ismail S, Koppstein D, Jang M, Hudson B, Sarafianos S, Tuske S, Patel J, Jansen R, Irschik H, Arnold E, Ebright RH.
The RNA polymerase "switch region" is a target for inhibitors.
Cell 135 2008 295-307 [PubMed: 18957204]
http://dx.doi.org/10.1016/j.cell.2008.09.033
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InterPro 23.1