The domain within your query sequence starts at position 17 and ends at position 139; the E-value for the RPR domain shown below is 6.74e-43.

DACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYL
MDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDV
RVN

RPR

RPR
SMART accession number:SM00582
Description: domain present in proteins, which are involved in regulation of nuclear pre-mRNA
Interpro abstract (IPR006569):

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. CTD recognition is dependent on the phosphorylation state of the CTD itself, which varies during the course of transcription but has also been linked to the isomerization state of the CTD's proline residues. Several RNA-processing factors recognise the CTD by means of a conserved CTD-interacting domain (CID). Factors with CID domains include the serine/arginine-rich-like factors SCAF4 and SCAF8, Nrd1 (which is implicated in polyadenylation-independent RNA 3'-end formation) and Pcf11. Pcf11 is a conserved and essential subunit of the yeast cleavage factor 1A, which is required for 3'-RNA processing and transcription termination [(PUBMED:15241417), (PUBMED:15665873)].

The CID domain is a right-handed superhelix of eight alpha-helices forming a compact domain. The CID fold closely resembles that of VHS domains IPR002014 and is related to armadillo-repeat proteins IPR000225, except for the two amino-terminal helices. Amino acid residues in the hydrophobic core of the domain are highly conserved across CID domains [(PUBMED:15241417), (PUBMED:15665873)].

Family alignment:
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There are 9580 RPR domains in 9578 proteins in SMART's nrdb database.

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