The domain within your query sequence starts at position 32 and ends at position 98; the E-value for the RNA_pol_L domain shown below is 4.2e-12.

LFTINKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAI
TDLISEL

RNA_pol_L

RNA_pol_L
PFAM accession number:PF01193
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)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry RNA_pol_L