The domain within your query sequence starts at position 60 and ends at position 255; the E-value for the RPOLD domain shown below is 9.13e-47.



RNA polymerases D
SMART accession number:SM00662
Description: DNA-directed RNA polymerase subunit D and bacterial alpha chain
Interpro abstract (IPR011263):

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 [ (PUBMED:10972792) ]. 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 [ (PUBMED:12860379) ]. 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 [ (PUBMED:12694606) ].

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 ( IPR011260 ).

GO process:transcription, DNA-templated (GO:0006351)
GO function:DNA-directed 5'-3' RNA polymerase activity (GO:0003899)
Family alignment:
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There are 23040 RPOLD domains in 23040 proteins in SMART's nrdb database.

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