histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and similar proteins; The family includes TAF9 (also called TATA Binding Protein (TBP) associated factor 9, RNA polymerase II TBP-associated factor subunit G, STAF31/32, transcription initiation factor TFIID 31 kDa subunit, TAFII-31, TAFII31, transcription initiation factor TFIID 32 kDa subunit, TAFII-32, or TAFII32) and TAF9-like (also called transcription initiation factor TFIID subunit 9B, neuronal cell death-related protein 7, DN-7, or transcription-associated factor TAFII31L), which are essential for cell viability. They are involved in transcriptional activation as well as the repression of distinct but overlapping sets of genes. They may have roles in gene regulation associated with apoptosis. Both TAF9 and TAF9-like are TAFs that are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16, and the basal transcription factor TFIIB.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1TAF_A       1 PKDAQVIMSILKELNVQEYEPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRLATEVTLD 68
Cdd:cd07979  1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRAD 68

histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and similar proteins; The family includes TAF9 (also called TATA Binding Protein (TBP) associated factor 9, RNA polymerase II TBP-associated factor subunit G, STAF31/32, transcription initiation factor TFIID 31 kDa subunit, TAFII-31, TAFII31, transcription initiation factor TFIID 32 kDa subunit, TAFII-32, or TAFII32) and TAF9-like (also called transcription initiation factor TFIID subunit 9B, neuronal cell death-related protein 7, DN-7, or transcription-associated factor TAFII31L), which are essential for cell viability. They are involved in transcriptional activation as well as the repression of distinct but overlapping sets of genes. They may have roles in gene regulation associated with apoptosis. Both TAF9 and TAF9-like are TAFs that are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16, and the basal transcription factor TFIIB.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1TAF_A       1 PKDAQVIMSILKELNVQEYEPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRLATEVTLD 68
Cdd:cd07979  1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRAD 68

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.

                       10        20        30        40        50        60
               ....*....|....*....|....*....|....*....|....*....|....*....|
1TAF_A       5 QVIMSILKELNVQEYEPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRLATE 64
Cdd:cd00076  4 SAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63

Bromodomain associated; This domain is predicted to bind DNA and is often found associated with pfam00439 and in transcription factors. It has a histone-like fold.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
1TAF_A         5 QVIMSILKELNVQEYEPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRLA 62
Cdd:pfam07524 10 VAVSQILEHAGFDSAEESALETLTDIAQSYIRELGEQAKSFAEHAGRSEPTLFDVVLT 67

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1TAF_A         20 EPRVVNQLLEFTFRYVTSILDDAKVYANHARKKTIDLDDVRL 61
Cdd:pfam15511  31 SKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVIL 72