1 Child Features
| DB identifier | Type | Name |
|---|---|---|
| IPR011263 | Domain | DNA-directed RNA polymerase, RpoA/D/Rpb3-type |
| Type: | Domain | Name: | DNA-directed RNA polymerase, RBP11-like dimerisation domain |
| Description: | RNA polymerase (RNAP) II, which is responsible for all mRNA synthesis in eukaryotes, consists of 12 subunits. Subunits Rpb3 and Rpb11 form a heterodimer that is functionally analogous to the archaeal RNAP D/L heterodimer, and the prokaryotic RNAP alpha subunit homodimer. In each case, they play a key role in RNAP assembly by forming a platform on which the catalytic subunits (eukaryotic Rpb1/Rpb2, and prokaryotic beta/beta') can interact []. These different subunits share regions of homology. Rpb11 contains a domain (Rpb11-like domain) that is required for dimerisation, and binds to a homologous region on Rpb3. The Rpb11-like domain in Rpb11 and archaeal L subunits is contiguous, whereas in Rpb3, archaeal D, and prokaryotic alpha subunits (), the Rpb11-like domain is interrupted by an insert domain (). In the prokaryotic RNAP alpha subunit, the Rpb11-like domain and the insert domain form two subregions of the N-terminal domain.The structure of the Rpb11-like domain consists of a two-layer alpha/beta fold consisting of beta(2)-alpha-beta(2)-alpha. Rpb3 and Rpb11 in yeast RNAP [, ] have been shown to share a high degree of sequence and structural similarity to the alpha subunit of bacterial RNAP [, ]. | Short Name: | RBP11-like_dimer |
| DB identifier | Type | Name |
|---|---|---|
| IPR011263 | Domain | DNA-directed RNA polymerase, RpoA/D/Rpb3-type |
