Summary: Transcription initiation factor IID, 31kD subunit
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Transcription initiation factor IID, 31kD subunit Provide feedback
This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.
Xie X, Kokubo T, Cohen SL, Mirza UA, Hoffmann A, Chait BT, Roeder RG, Nakatani Y, Burley SK; , Nature 1996;380:316-322.: Structural similarity between TAFs and the heterotetrameric core of the histone octamer. PUBMED:8598927 EPMC:8598927
Internal database links
|Similarity to PfamA using HHSearch:||Histone Bromo_TP CENP-S|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003162Human 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].
TAFII-31 protein is a transcriptional coactivator of the p53 protein [PUBMED:7761466].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||transcription initiation, DNA-dependent (GO:0006352)|
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Members of this clan all possess a histone fold. Generally proteins in this clan are DNA binding.
The clan contains the following 11 members:Bromo_TP CBFD_NFYB_HMF CENP-S CENP-T CENP-W Histone TAF TAFII28 TFIID-18kDa TFIID-31kDa TFIID_20kDa
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Curation and family details
|Seed source:||Pfam-B_6729 (release 5.2)|
|Author:||Mian N, Bateman A|
|Number in seed:||5|
|Number in full:||368|
|Average length of the domain:||121.40 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||53.69 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TFIID-31kDa domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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