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132  structures 584  species 2  interactions 1985  sequences 8  architectures

Family: TBP (PF00352)

Summary: Transcription factor TFIID (or TATA-binding protein, TBP)

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "TATA-binding protein". More...

TATA-binding protein Edit Wikipedia article

TBP
PDB 1ngm EBI.jpg
crystal structure of a yeast brf1-tbp-dna ternary complex
Identifiers
Symbol TBP
Pfam PF00352
Pfam clan CL0407
InterPro IPR000814
PROSITE PDOC00303
SCOP 1tbp
SUPERFAMILY 1tbp
TATA box binding protein

PDB rendering based on 1c9b.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TBP; GTF2D; GTF2D1; HDL4; SCA17; TFIID
External IDs OMIM600075 MGI101838 HomoloGene2404 GeneCards: TBP Gene
RNA expression pattern
PBB GE TBP 203135 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6908 21374
Ensembl ENSG00000112592 ENSMUSG00000014767
UniProt P20226 P29037
RefSeq (mRNA) NM_001172085 NM_013684
RefSeq (protein) NP_001165556 NP_038712
Location (UCSC) Chr 6:
170.86 – 170.88 Mb
Chr 17:
15.5 – 15.53 Mb
PubMed search [1] [2]

The TATA-binding protein (TBP) is a general transcription factor that binds specifically to a DNA sequence called the TATA box. This DNA sequence is found about 30 base pairs upstream of the transcription start site in some eukaryotic gene promoters.[1] TBP, along with a variety of TBP-associated factors, make up the TFIID, a general transcription factor that in turn makes up part of the RNA polymerase II preinitiation complex.[2] As one of the few proteins in the preinitiation complex that binds DNA in a sequence-specific manner, it helps position RNA polymerase II over the transcription start site of the gene. However, it is estimated that only 10-20% of human promoters have TATA boxes. Therefore, TBP is probably not the only protein involved in positioning RNA polymerase II.

TBP is involved in DNA melting (double strand separation) by bending the DNA by 80° (the AT-rich sequence to which it binds facilitates easy melting). The TBP is an unusual protein in that it binds the minor groove using a β sheet.

Another distinctive feature of TBP is a long string of glutamines in the N-terminus of the protein. This region modulates the DNA binding activity of the C-terminus, and modulation of DNA-binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this polyglutamine tract, and thus increase the length of the polyglutamine string, are associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease.[3]

Role as Transcription Factor Subunit[edit]

TBP is a subunit of the eukaryotic transcription factor TFIID. TFIID is the first protein to bind to DNA during the formation of the pre-initiation transcription complex of RNA polymerase II (RNA Pol II). Binding of TFIID to the TATA box in the promoter region of the gene initiates the recruitment of other factors required for RNA Pol II to begin transcription. Some of the other recruited transcription factors include TFIIA, TFIIB, and TFIIF. Each of these transcription factors is formed from the interaction of many protein subunits, indicating that transcription is a heavily regulated process.

TBP is also a necessary component of RNA polymerase I and RNA polymerase III, and is, it is thought, the only common subunit required by all three of the RNA polymerases.

DNA-Protein Interactions[edit]

When TBP binds to a TATA box within the DNA, it distorts the DNA by inserting amino acid side-chains between base pairs, partially unwinding the helix, and doubly kinking it. The distortion is accomplished through a great amount of surface contact between the protein and DNA. TBP binds with the negatively charged phosphates in the DNA backbone through positively charged lysine and arginine amino acid residues. The sharp bend in the DNA is produced through projection of four bulky phenylalanine residues into the minor groove. As the DNA bends, its contact with TBP increases, thus enhancing the DNA-protein interaction.

The strain imposed on the DNA through this interaction initiates melting, or separation, of the strands. Because this region of DNA is rich in adenine and thymine residues, which base-pair through only two hydrogen bonds, the DNA strands are more easily separated. Separation of the two strands exposes the bases and allows RNA polymerase II to begin transcription of the gene.

TBP's C-terminus composes of a helicoidal shape that (incompletely) complements the T-A-T-A region of DNA. It is interesting to note that this incompleteness allows DNA to be passively bent on binding.

For information on the use of TBP in cells see: RNA polymerase I, RNA polymerase II, and RNA polymerase III.

Interactions[edit]

TATA-binding protein has been shown to interact with:


Complex Assembly[edit]

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.[41][42] 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.[43]

Structure[edit]

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 .[44] By contrast, the N-terminal region varies in both length and sequence.

References[edit]

  1. ^ Kornberg RD (2007). "The molecular basis of eukaryotic transcription". Proc. Natl. Acad. Sci. U.S.A. 104 (32): 12955–61. doi:10.1073/pnas.0704138104. PMC 1941834. PMID 17670940. 
  2. ^ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annu. Rev. Genet. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823. 
  3. ^ "Entrez Gene: TBP TATA box binding protein". 
  4. ^ McCulloch V, Hardin P, Peng W, Ruppert JM, Lobo-Ruppert SM (August 2000). "Alternatively spliced hBRF variants function at different RNA polymerase III promoters". EMBO J. 19 (15): 4134–43. doi:10.1093/emboj/19.15.4134. PMC 306597. PMID 10921893. 
  5. ^ Wang Z, Roeder RG (July 1995). "Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7026–30. doi:10.1073/pnas.92.15.7026. PMC 41464. PMID 7624363. 
  6. ^ a b c d Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119. 
  7. ^ Chicca JJ, Auble DT, Pugh BF (March 1998). "Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1". Mol. Cell. Biol. 18 (3): 1701–10. PMC 108885. PMID 9488487. 
  8. ^ Metz R, Bannister AJ, Sutherland JA, Hagemeier C, O'Rourke EC, Cook A, Bravo R, Kouzarides T (September 1994). "c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein". Mol. Cell. Biol. 14 (9): 6021–9. doi:10.1128/MCB.14.9.6021. PMC 359128. PMID 8065335. 
  9. ^ Franklin CC, McCulloch AV, Kraft AS (February 1995). "In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB". Biochem. J. 305 (3): 967–74. PMC 1136352. PMID 7848298. 
  10. ^ Brendel C, Gelman L, Auwerx J (June 2002). "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism". Mol. Endocrinol. 16 (6): 1367–77. doi:10.1210/me.16.6.1367. PMID 12040021. 
  11. ^ Mariotti M, De Benedictis L, Avon E, Maier JA (August 2000). "Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo". J. Biol. Chem. 275 (31): 24047–51. doi:10.1074/jbc.M001928200. PMID 10816571. 
  12. ^ Kabe Y, Goto M, Shima D, Imai T, Wada T, Morohashi K, Shirakawa M, Hirose S, Handa H (November 1999). "The role of human MBF1 as a transcriptional coactivator". J. Biol. Chem. 274 (48): 34196–202. doi:10.1074/jbc.274.48.34196. PMID 10567391. 
  13. ^ a b Tang H, Sun X, Reinberg D, Ebright RH (February 1996). "Protein-protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex". Proc. Natl. Acad. Sci. U.S.A. 93 (3): 1119–24. doi:10.1073/pnas.93.3.1119. PMC 40041. PMID 8577725. 
  14. ^ Bushnell DA, Westover KD, Davis RE, Kornberg RD (February 2004). "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms". Science 303 (5660): 983–8. doi:10.1126/science.1090838. PMID 14963322. 
  15. ^ DeJong J, Bernstein R, Roeder RG (April 1995). "Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3313–7. doi:10.1073/pnas.92.8.3313. PMC 42156. PMID 7724559. 
  16. ^ Ozer J, Mitsouras K, Zerby D, Carey M, Lieberman PM (June 1998). "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem. 273 (23): 14293–300. doi:10.1074/jbc.273.23.14293. PMID 9603936. 
  17. ^ Sun X, Ma D, Sheldon M, Yeung K, Reinberg D (October 1994). "Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription". Genes Dev. 8 (19): 2336–48. doi:10.1101/gad.8.19.2336. PMID 7958900. 
  18. ^ Ruppert S, Tjian R (November 1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. 9 (22): 2747–55. doi:10.1101/gad.9.22.2747. PMID 7590250. 
  19. ^ Malik S, Guermah M, Roeder RG (March 1998). "A dynamic model for PC4 coactivator function in RNA polymerase II transcription". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2192–7. doi:10.1073/pnas.95.5.2192. PMC 19292. PMID 9482861. 
  20. ^ a b Thut CJ, Goodrich JA, Tjian R (August 1997). "Repression of p53-mediated transcription by MDM2: a dual mechanism". Genes Dev. 11 (15): 1974–86. doi:10.1101/gad.11.15.1974. PMC 316412. PMID 9271120. 
  21. ^ Léveillard T, Wasylyk B (December 1997). "The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter". J. Biol. Chem. 272 (49): 30651–61. doi:10.1074/jbc.272.49.30651. PMID 9388200. 
  22. ^ Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R (May 1999). "Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300)". Biochem. J. 339 (3): 751–8. doi:10.1042/0264-6021:3390751. PMC 1220213. PMID 10215616. 
  23. ^ Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C (May 1997). "Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism". Mol. Cell. Biol. 17 (5): 2920–32. PMC 232144. PMID 9111364. 
  24. ^ Zhang H, Catron KM, Abate-Shen C (March 1996). "A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1764–9. doi:10.1073/pnas.93.5.1764. PMC 39855. PMID 8700832. 
  25. ^ a b c d e f g h Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (June 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318. 
  26. ^ Seto E, Usheva A, Zambetti GP, Momand J, Horikoshi N, Weinmann R, Levine AJ, Shenk T (December 1992). "Wild-type p53 binds to the TATA-binding protein and represses transcription". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12028–32. doi:10.1073/pnas.89.24.12028. PMC 50691. PMID 1465435. 
  27. ^ a b Cvekl A, Kashanchi F, Brady JN, Piatigorsky J (June 1999). "Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein". Invest. Ophthalmol. Vis. Sci. 40 (7): 1343–50. PMID 10359315. 
  28. ^ Zwilling S, Annweiler A, Wirth T (May 1994). "The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP". Nucleic Acids Res. 22 (9): 1655–62. doi:10.1093/nar/22.9.1655. PMC 308045. PMID 8202368. 
  29. ^ Guermah M, Malik S, Roeder RG (June 1998). "Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1". Mol. Cell. Biol. 18 (6): 3234–44. PMC 108905. PMID 9584164. 
  30. ^ Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA (March 1995). "Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators". J. Biol. Chem. 270 (13): 7219–26. doi:10.1074/jbc.270.13.7219. PMID 7706261. 
  31. ^ Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (August 1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283. 
  32. ^ Siegert JL, Robbins PD (January 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. 19 (1): 846–54. PMC 83941. PMID 9858607. 
  33. ^ a b c d Ruppert S, Wang EH, Tjian R (March 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature 362 (6416): 175–9. doi:10.1038/362175a0. PMID 7680771. 
  34. ^ O'Brien T, Tjian R (May 1998). "Functional analysis of the human TAFII250 N-terminal kinase domain". Mol. Cell 1 (6): 905–11. doi:10.1016/S1097-2765(00)80089-1. PMID 9660973. 
  35. ^ a b c Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell. Sci. 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. PMID 12665565. 
  36. ^ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (March 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. 272 (10): 6714–21. doi:10.1074/jbc.272.10.6714. PMID 9045704. 
  37. ^ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Mol. Cell. Biol. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863. 
  38. ^ a b Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I (April 1995). "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID". EMBO J. 14 (7): 1520–31. PMC 398239. PMID 7729427. 
  39. ^ May M, Mengus G, Lavigne AC, Chambon P, Davidson I (June 1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. PMC 450252. PMID 8670810. 
  40. ^ Hoffmann A, Roeder RG (July 1996). "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. 271 (30): 18194–202. doi:10.1074/jbc.271.30.18194. PMID 8663456. 
  41. ^ Hochheimer A, Tjian R (June 2003). "Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression". Genes Dev. 17 (11): 1309–20. doi:10.1101/gad.1099903. PMID 12782648. 
  42. ^ Pugh BF (September 2000). "Control of gene expression through regulation of the TATA-binding protein". Gene 255 (1): 1–14. PMID 10974559. 
  43. ^ Davidson I (July 2003). "The genetics of TBP and TBP-related factors". Trends Biochem. Sci. 28 (7): 391–8. doi:10.1016/S0968-0004(03)00117-8. PMID 12878007. 
  44. ^ Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK (November 1992). "Crystal structure of TFIID TATA-box binding protein". Nature 360 (6399): 40–6. doi:10.1038/360040a0. PMID 1436073. 

External links[edit]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Transcription factor TFIID (or TATA-binding protein, TBP) Provide feedback

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Literature references

  1. 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 EPMC:1436073

  2. 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 EPMC:8598932

  3. 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 EPMC:2374612

  4. Gasch A, Hoffmann A, Horikoshi M, Roeder RG, Chua NH; , Nature 1990;346:390-394.: Arabidopsis thaliana contains two genes for TFIID. PUBMED:2197561 EPMC:2197561


Internal database links

External database links

This tab holds annotation information from the InterPro database.

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.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan TBP-like (CL0407), which has the following description:

TBP is a transcription factor whose DNA binding fold is composed of a curved antiparallel beta-sheet [1]. This fold is also found in the N terminal region of DNA repair glycosylases. The N terminal domain of DNA glycosylase has only a single copy of the fold, whereas TBP contains a duplication of this fold [2-3].

The clan contains the following 3 members:

AlkA_N OGG_N TBP

Alignments

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  Seed
(135)
Full
(1985)
Representative proteomes NCBI
(1872)
Meta
(373)
RP15
(351)
RP35
(608)
RP55
(909)
RP75
(1141)
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  Seed
(135)
Full
(1985)
Representative proteomes NCBI
(1872)
Meta
(373)
RP15
(351)
RP35
(608)
RP55
(909)
RP75
(1141)
Alignment:
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Sequence:
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  Seed
(135)
Full
(1985)
Representative proteomes NCBI
(1872)
Meta
(373)
RP15
(351)
RP35
(608)
RP55
(909)
RP75
(1141)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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 HMMER3.

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's seed alignment. 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 alignment.

Note: You can also download the data file for the tree.

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 View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD
Number in seed: 135
Number in full: 1985
Average length of the domain: 83.40 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 62.81 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.9 22.9
Trusted cut-off 23.1 23.0
Noise cut-off 22.7 22.8
Model length: 86
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

TBP TFIIA_gamma_C

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 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 TBP domain has been found. There are 132 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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