Summary
Transcription factor TFIID (or TATA-binding protein, TBP)
No Pfam abstract.
Literature references
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Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK; , Nature 1992;360:40-46.: Crystal structure of TFIID TATA-box binding protein. PUBMED:1436073
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Hoffmann A, Chiang CM, Oelgeschlager T, Xie X, Burley SK, Nakatani Y, Roeder RG; , Nature 1996;380:356-359.: A histone octamer-like structure within TFIID. PUBMED:8598932
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Hoffman A, Sinn E, Yamamoto T, Wang J, Roy A, Horikoshi M, Roeder RG; , Nature 1990;346:387-390.: Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID). PUBMED:2374612
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Gasch A, Hoffmann A, Horikoshi M, Roeder RG, Chua NH; , Nature 1990;346:390-394.: Arabidopsis thaliana contains two genes for TFIID. PUBMED:2197561
InterPro entry IPR000814
The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box PUBMED:12782648, PUBMED:10974559. TBP associates with a host of factors, including the general transcription factors TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins PUBMED:12878007.
The C-terminal core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box and interacts with transcription factors and regulatory proteins PUBMED:1436073. By contrast, the N-terminal region varies in both length and sequence.
Clan
This family is a member of clan TBP-like (CL0407), which contains the following 3 members:
AlkA_N OGG_N TBPGene Ontology
| Cellular component | nucleus (GO:0005634) |
| transcription factor TFIID complex (GO:0005669) | |
| Molecular function | DNA binding (GO:0003677) |
| RNA polymerase II transcription factor activity (GO:0003702) | |
| Biological process | regulation of transcription, DNA-dependent (GO:0006355) |
| transcription initiation from RNA polymerase II promoter (GO:0006367) |
External database links
| HOMSTRAD: | tbpc |
| PANDIT: | PF00352 |
| PROSITE: | PDOC00303 |
| SCOP: | 1tbp |
| SYSTERS: | TBP |
| External sites: | 1 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD |
| Number in seed: | 138 |
| Number in full: | 1042 |
| Average length of the domain: | 83.40 aa |
| Average identity of full alignment: | 36 % |
| Average coverage of the sequence by the domain: | 31.60 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 86 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 TBP domain has been found.
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