SMART: Pfam domain TFIID-31kDa

The domain within your query sequence starts at position 2 and ends at position 130; the E-value for the TFIID-31kDa domain shown below is 3.8e-62.

ESGKMASPKSMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHA
KKATVDADDVRLAIQCRADQSFTSPPPRDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYC
LTAPNYRLK

TFIID-31kDa

PFAM accession number:	PF02291
Interpro abstract (IPR003162):	Human transcription initiation factor TFIID is composed of the TATA-binding polypeptide (TBP) and at least 13 TBP-associated factors (TAFs) that collectively or individually are involved in activator-dependent transcription [ (PUBMED:7667268) (PUBMED:19308322) (PUBMED:11963920) ]. This entry represents the N terminus of the 31kDa subunit (42kDa in Drosophila) of transcription initiation factor IID (TAFII31), also known as transcription initiation factor TFIID subunit 9 (TAF9). It has been shown that TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16 and the basal transcription factor TFIIB. Binding to p53 is an essential requirement for p53 mediated transcription activation. TAF9 is a component other TBP-free TAF complexes containing the GCN5-type histone acetyltransferase. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFS and many other transcription factors. TFIID has a histone octamer-like substructure. TFIID has a histone octamer-like substructure. TAF9 is a shared subunit of both, histone acetyltransferase complex (SAGA) and TFIID complexes. TAF9 domain interacts with TAF6 to form a novel histone-like heterodimer that is structurally related to the histone H3 and H4 oligomer [ (PUBMED:8598927) (PUBMED:11295558) (PUBMED:10664584) (PUBMED:15899866) ].
GO process:	DNA-templated transcription, initiation (GO:0006352)

PFAM accession number:

PF02291

Interpro abstract (IPR003162):

Human transcription initiation factor TFIID is composed of the TATA-binding polypeptide (TBP) and at least 13 TBP-associated factors (TAFs) that collectively or individually are involved in activator-dependent transcription [ (PUBMED:7667268) (PUBMED:19308322) (PUBMED:11963920) ]. This entry represents the N terminus of the 31kDa subunit (42kDa in Drosophila) of transcription initiation factor IID (TAFII31), also known as transcription initiation factor TFIID subunit 9 (TAF9). It has been shown that TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16 and the basal transcription factor TFIIB. Binding to p53 is an essential requirement for p53 mediated transcription activation.

TAF9 is a component other TBP-free TAF complexes containing the GCN5-type histone acetyltransferase. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFS and many other transcription factors. TFIID has a histone octamer-like substructure. TFIID has a histone octamer-like substructure. TAF9 is a shared subunit of both, histone acetyltransferase complex (SAGA) and TFIID complexes. TAF9 domain interacts with TAF6 to form a novel histone-like heterodimer that is structurally related to the histone H3 and H4 oligomer [ (PUBMED:8598927) (PUBMED:11295558) (PUBMED:10664584) (PUBMED:15899866) ].

GO process:

DNA-templated transcription, initiation (GO:0006352)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TFIID-31kDa