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InterPro: IPR000722 RNA polymerase, alpha subunit

Protein matches Help

UniProtKB

Matches:

5791 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000722 RNA_pol_asu

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.40.40.30	RNA_pol_A	5256
Pfam	PF00623	RNA_pol_Rpb1_2	5788
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006592 RNA polymerase, N-terminal
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

GO Term annotation Help

Process

GO:0006350 transcription

Function

GO:0003677 DNA binding
GO:0003899 DNA-directed RNA polymerase activity

InterPro annotation

Entry Details in BioMart

Abstract

RNA polymerases catalyse the DNA dependent polymerisation of RNA from DNA, using the four ribonucleoside triphosphates as substrates. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial and chloroplast polymerases). Eukaryotic RNA polymerase I is essentially used to transcribe ribosomal RNA units, polymerase II is used for mRNA precursors, and III is used to transcribe 5S and tRNA genes. Each class of RNA polymerase is assembled from nine to fourteen different polypeptides. Members of the family include the largest subunit from eukaryotes; the gamma subunit from Cyanobacteria; the beta' subunit from bacteria; the A' subunit from archaea; and the B'' subunit from chloroplast RNA polymerases.

Structural links Help

PDB - click here

SCOP: e.29.1.2 , i.8.1.1

Database links Help

Enzyme: EC:2.7.7.6

PANDIT: PF00623

Blocks: IPB000722

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000722

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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

Publications Help

Additional Reading Open in usermanual
	Vassylyev DG, Vassylyeva MN, Perederina A, Tahirov TH, Artsimovitch I. Structural basis for transcription elongation by bacterial RNA polymerase. Nature 448 2007 157-62 [PubMed: 17581590] http://dx.doi.org/10.1038/nature05932
	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
	Severinov K, Mustaev A, Kukarin A, Muzzin O, Bass I, Darst SA, Goldfarb A. Structural modules of the large subunits of RNA polymerase. Introducing archaebacterial and chloroplast split sites in the beta and beta' subunits of Escherichia coli RNA polymerase. J. Biol. Chem. 271 1996 27969-74 [PubMed: 8910400] http://dx.doi.org/10.1074/jbc.271.44.27969
	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
	Cramer P, Bushnell DA, Kornberg RD. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292 2001 1863-76 [PubMed: 11313498] http://dx.doi.org/10.1126/science.1059493
	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

InterPro 23.1