|PROSITE documentation PDOC51391
CID domain profile
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 recognize 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 [1,2].
The CID domain is a right-handed superhelix of eight α-helices forming a
compact domain (see <PDB:1SZ9>). The CID fold closely resembles that of VHS
domains (see <PDOC50179>) and is related to armadillo-repeat proteins (see
(<PDOC50176>), except for the two amino-terminal helices. Amino acid residues
in the hydrophobic core of the domain are highly conserved across CID domains
The profile we developed covers the entire CID domain.
June 2008 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|CID, PS51391; CID domain profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1SZ9 1SZA 2BF0 2DIW ... [ALL]
||Meinhart A., Cramer P.
||Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors.
||Noble C.G., Hollingworth D., Martin S.R., Ennis-Adeniran V., Smerdon S.J., Kelly G., Taylor I.A., Ramos A.
||Key features of the interaction between Pcf11 CID and RNA polymerase II CTD.
||Nat. Struct. Mol. Biol. 12:144-151(2005).
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