1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR009025 | Domain | DNA-directed RNA polymerase, RBP11-like dimerisation domain |
| Type: | Domain | Name: | DNA-directed RNA polymerase, RpoA/D/Rpb3-type |
| Description: | The core of the bacterial RNA polymerase (RNAP) consists of four subunits, two alpha, a beta and a beta', which are conserved from bacteria to mammals. The alpha subunit (RpoA) initiates RNAP assembly by dimerising to form a platform on which the beta subunits can interact, and plays a direct role in promoter recognition []. In eukaryotes, RNA polymerase (RNAP) II is responsible for all mRNA synthesis. RNAP-II consists of 12 subunits, where subunits Rpb3 and Rpb11 form a heterodimer that is functionally analogous to the bacterial RpoA homodimer []. Archaeal RNAP closely resembles eukaryotic RNAP-II, and is composed of 12 subunits, of which D and L form a heterodimer resembling the Rpb3/Rpb11 and RpoA/RpoA dimers [].The bacterial RpoA, eukaryotic Rpb3 and archaeal D subunits share sequence and structural motifs, and can be placed into a single family. These subunits also have unique sequence motifs, especially at their C-terminal ends, which are involved in promoter specificity, for example the CTD of the bacterial RNAP alpha subunit (). | Short Name: | DNA-dir_RNA_pol_RpoA/D/Rpb3 |
| DB identifier | Type | Name |
|---|---|---|
| IPR009025 | Domain | DNA-directed RNA polymerase, RBP11-like dimerisation domain |
