Protein Domain : IPR010243

Type:  Family Name:  DNA-directed RNA polymerase, beta subunit
Description:  DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerases are multimeric enzymes and are composed of a variable number of subunits. The core RNA polymerase complex consists of five subunits (two alpha, one beta, one beta-prime and one omega) and is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with the core RNA polymerase complex to form a holoenzyme []. The core RNA polymerase complex forms a "crab claw"-like structure with an internal channel running along the full length []. The key functional sites of the enzyme, as defined by mutational and cross-linking analysis, are located on the inner wall of this channel.RNA synthesis follows after the attachment of RNA polymerase to a specific site, the promoter, on the template DNA strand. The RNA synthesis process continues until a termination sequence is reached. The RNA product, which is synthesised in the 5' to 3'direction, is known as the primary transcript. Eukaryotic nuclei contain three distinct types of RNA polymerases that differ in the RNA they synthesise:RNA polymerase I: located in the nucleoli, synthesises precursors of most ribosomal RNAs.RNA polymerase II: occurs in the nucleoplasm, synthesises mRNA precursors. RNA polymerase III: also occurs in the nucleoplasm, synthesises the precursors of 5S ribosomal RNA, the tRNAs, and a variety of other small nuclear and cytosolic RNAs. Eukaryotic cells are also known to contain separate mitochondrial and chloroplast RNA polymerases. Eukaryotic RNA polymerases, whose molecular masses vary in size from 500 to 700 kDa, contain two non-identical large (>100 kDa) subunits and an array of up to 12 different small (less than 50 kDa) subunits.This entry describes orthologues of the beta subunit of bacterial RNA polymerase. The core enzyme consists of two alpha chains, one beta chain, and one beta' subunit. Short Name:  DNA-dir_RNA_pol_bsu
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0 Child Features

8 Contains

DB identifier Type Name
IPR007120 Domain DNA-directed RNA polymerase, subunit 2, domain 6
IPR007641 Domain RNA polymerase Rpb2, domain 7
IPR007645 Domain RNA polymerase Rpb2, domain 3
IPR007642 Domain RNA polymerase Rpb2, domain 2
IPR007644 Domain RNA polymerase, beta subunit, protrusion
IPR014724 Domain RNA polymerase Rpb2, OB-fold
IPR019462 Domain DNA-directed RNA polymerase, beta subunit, external 1 domain
IPR007121 Conserved_site RNA polymerase, beta subunit, conserved site

2 Cross Referencess

Identifier
TIGR02013
MF_01321

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0003677 IPR010243
GO:0003899 IPR010243
GO:0006351 IPR010243

3 Ontology Annotations

GO Term Gene Name
GO:0003677 IPR010243
GO:0003899 IPR010243
GO:0006351 IPR010243

1 Parent Features

DB identifier Type Name
IPR015712 Family DNA-directed RNA polymerase, subunit 2

9 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0290.1.p PAC:28856332 Arabidopsis halleri 1342  
Brdisv1pangenome1000469m.p PAC:33659434 Brachypodium distachyon Pangenome 1116  
Brdisv1pangenome1008423m.p PAC:33658554 Brachypodium distachyon Pangenome 1043  
Brdisv1pangenome1008737m.p PAC:33658924 Brachypodium distachyon Pangenome 942  
Brdisv1BdTR8i1044373m.p PAC:34241207 Brachypodium distachyon BdTR8i 947  
Brdisv1BdTR12c1005918m.p PAC:34395586 Brachypodium distachyon BdTR12c 1117  
Brdisv1BdTR11G1006490m.p PAC:34616052 Brachypodium distachyon BdTR11g 1105  
Brdisv1BdTR11A1044836m.p PAC:35696535 Brachypodium distachyon BdTR11a 1612  
Brdisv1BdTR11A1044130m.p PAC:35689044 Brachypodium distachyon BdTR11a 1043  

2 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3052291
            10499798