Summary: Transcription initiation factor IID, 31kD subunit
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
|SCOOP:||TAF UPF0137 TFIID_20kDa TAFII28 Bromo_TP XisI DUF1931 CENP-T_C CENP-S HIGH_NTase1_ass Bromo_TP_like|
|Similarity to PfamA using HHSearch:||Histone Bromo_TP CENP-T_C CENP-S|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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]. 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. It TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||DNA-templated transcription, initiation (GO:0006352)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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- the UniProt description of the protein sequence
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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 13 members:Bromo_TP Bromo_TP_like CBFD_NFYB_HMF CENP-S CENP-T_C CENP-W CENP-X Histone TAF TAFII28 TFIID-18kDa TFIID-31kDa TFIID_20kDa
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_6729 (release 5.2)|
|Author:||Mian N, Bateman A|
|Number in seed:||101|
|Number in full:||683|
|Average length of the domain:||122.30 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||54.49 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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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