The domain within your query sequence starts at position 9 and ends at position 468; the E-value for the TFIIA domain shown below is 6.87e-202.

KLYQSVIEDVIEGVRDLFAEEGIEEQVLKDLKKLWETKVLQSKATEDFFRNSTQVPLLTL
QLPHALPPALQPEASLLIPAGRTLPSFTPEDLNTANCGANFAFAGYPIHVPAGMAFQTAS
GHLYKVNVPVMVTQTSGRTEILQHPFQQVLQQLGQPLVIQTTVPTLHPCSLQAATEKSLR
MEAVLQPPPILHPPPVDRTHVENAASDRRLLPGNELRPQESSPYLSLPGVGFPPQAALTE
SSLEPVLGVSASLTQNLHSDPFSQGPPGPLHHHLLESQLQSLKDSIYGCDSTKQLRKAEE
PSSLRVSEKNCTSERDLNIRVTDDDINEIIQIDGTGDNSSTEEMGSIRDADENEFPGIID
AGDLNVLEEVDSVSNEDSTANSSDNEDHQINAPEEDPLNSGDDVSEQDVPDLFDTENVIV
CQYDKIHRSKNRWKFYLKDGVMCFGGRDYVFAKAIGEAEW

TFIIA

Transcription factor IIA, alpha/beta subunit
TFIIA
SMART accession number:SM01371
Description: Transcription initiation factor IIA (TFIIA) is a heterotrimer, the three subunits being known as alpha, beta, and gamma, in order of molecular weight. This family represents the precursor that yields both the alpha and beta subunits. The TFIIA heterotrimer is an essential general transcription initiation factor for the expression of genes transcribed by RNA polymerase II. Together with TFIID, TFIIA binds to the promoter region; this is the first step in the formation of a pre-initiation complex (PIC). Binding of the rest of the transcription machinery follows this step (PMID:11089979). After initiation, the PIC does not completely dissociate from the promoter. Some components, including TFIIA, remain attached and re-initiate a subsequent round of transcription.
Interpro abstract (IPR004855):

Transcription factor IIA (TFIIA) is one of several factors that form part of a transcription pre-initiation complex along with RNA polymerase II, the TATA-box-binding protein (TBP) and TBP-associated factors, on the TATA-box sequence upstream of the initiation start site. After initiation, some components of the pre-initiation complex (including TFIIA) remain attached and re-initiate a subsequent round of transcription. TFIIA binds to TBP to stabilise TBP binding to the TATA element. TFIIA also inhibits the cytokine HMGB1 (high mobility group 1 protein) binding to TBP [(PUBMED:12818428)], and can dissociate HMGB1 already bound to TBP/TATA-box.

Human and Drosophila TFIIA have three subunits: two large subunits, LN/alpha and LC/beta, derived from the same gene, and a small subunit, S/gamma. Yeast TFIIA has two subunits: a large TOA1 subunit that shows sequence similarity to the N-terminal of LN/alpha and the C-terminal of LC/beta, and a small subunit, TOA2 that is highly homologous with S/gamma. The conserved regions of the large and small subunits of TFIIA combine to form two domains: a four-helix bundle (helical domain) composed of two helices from each of the N-terminal regions of TOA1 and TOA2 in yeast; and a beta-barrel (beta-barrel domain) composed of beta-sheets from the C-terminal regions of TOA1 and TOA2 [(PUBMED:8610010)].

This entry represents the precursor that yields both the alpha and beta subunits of TFIIA. The TFIIA heterotrimer is an essential general transcription initiation factor for the expression of genes transcribed by RNA polymerase II [(PUBMED:11089979)].

GO process:transcription initiation from RNA polymerase II promoter (GO:0006367)
GO component:transcription factor TFIIA complex (GO:0005672)
Family alignment:
View or

There are 2004 TFIIA domains in 2003 proteins in SMART's nrdb database.

Click on the following links for more information.