SMART: Pfam domain TFIIE-A

The domain within your query sequence starts at position 354 and ends at position 440; the E-value for the TFIIE-A_C domain shown below is 9.9e-36.

SESETSESDDDSPPRPAAAAPPHHHRDEDEEDEEFEEVADDPIVMVAGCPFSYSEVSQRP
ELVAQMTPEEKEAYIAMGQRMFEDLFE

TFIIE-A_C

PFAM accession number:	PF11521
Interpro abstract (IPR021600):	TFIIE is compiled of two subunits, alpha and beta. This entry represents the C-terminal domain of the alpha subunit. The alpha subunit is the largest and contains several functional domains which are important for basal transcription and cell growth. The C-terminal end of the protein binds directly to the amino-terminal PH domain of p62/Tfb1 (of IIH) which is involved in the recruitment of the general transcription factor IIH to the transcription preinitiation complex. p53 competes for the same binding site as TFIIE alpha, which shows their structural similarity. Like p53, the C terminus of TFIIE alpha (residues 336-439) can activate transcription in vivo [ (PUBMED:18160537) ].

PFAM accession number:

PF11521

Interpro abstract (IPR021600):

TFIIE is compiled of two subunits, alpha and beta. This entry represents the C-terminal domain of the alpha subunit. The alpha subunit is the largest and contains several functional domains which are important for basal transcription and cell growth. The C-terminal end of the protein binds directly to the amino-terminal PH domain of p62/Tfb1 (of IIH) which is involved in the recruitment of the general transcription factor IIH to the transcription preinitiation complex. p53 competes for the same binding site as TFIIE alpha, which shows their structural similarity. Like p53, the C terminus of TFIIE alpha (residues 336-439) can activate transcription in vivo [ (PUBMED:18160537) ].

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