The domain within your query sequence starts at position 373 and ends at position 601; the E-value for the RPOL_N domain shown below is 6.27e-50.

YQQLHVELSSSVCVQSVEKAPVMSKEVIEARKTLQALREQWEVELLRVLRETKATMGRQA
YEGQPTLYPFLCLLSEGEFVSILMQVLKVLPAQGEPLIQLAHNLGLRVLNRHLVKQKQVT
NHVQKLGQRYSQYLQLLASDTQVGILKPHPAFTHLLETAAEPTLTFETTEVPMLCPPLPW
TSLHSGAYLLSSTKLMRATEGTTQHQRLLEQCPPAQLHGPLDALTQLGN

RPOL_N

DNA-directed RNA polymerase N-terminal
RPOL_N
SMART accession number:SM01311
Description: This is the N-terminal domain of DNA-directed RNA polymerase. This domain has a role in interaction with regions of upstream promoter DNA and the nascent RNA chain, leading to the processivity of the enzyme PMID:9670025. In order to make mRNA transcripts the RNA polymerase undergoes a transition from the initiation phase (which only makes short fragments of RNA) to an elongation phase. This domain undergoes a structural change in the transition from initiation to elongation phase. The structural change results in abolition of the promoter binding site, creation of a channel accommodating the heteroduplex in the active site and formation of an exit tunnel which the RNA transcript passes through after peeling off the heteroduplex PMID:12242451.
Interpro abstract (IPR029262):

This is the N-terminal domain of DNA-directed RNA polymerase. This domain has a role in interaction with regions of upstream promoter DNA and the nascent RNA chain, leading to the processivity of the enzyme [ (PUBMED:9670025) ]. In order to make mRNA transcripts the RNA polymerase undergoes a transition from the initiation phase (which only makes short fragments of RNA) to an elongation phase. This domain undergoes a structural change in the transition from initiation to elongation phase. The structural change results in abolition of the promoter binding site, creation of a channel accommodating the heteroduplex in the active site, and formation of an exit tunnel which the RNA transcript passes through after peeling off the heteroduplex [ (PUBMED:12242451) ].

Family alignment:
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There are 2414 RPOL_N domains in 2413 proteins in SMART's nrdb database.

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