Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.

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gi 1958672853  51 LCSHTMMLPTRGQLEGRMIVTAYEHGLDN-VTEEAVSAVVYAVENHLKDILTSVVSR 106
Cdd:pfam12767  78 LAYESGELPDTDSLRKRMEPIAYEHGLVGgVSADCANLLNNALDVYLKNLLESCIDL 134

histone-fold domain found in transcriptional coactivator HFI1, transcriptional adapter 1 (TADA1), and similar proteins; This subfamily includes HFI1 and TADA1. HFI1, also called ADA1, is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TATA binding protein (TBP) interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA (SAGA altered, SPT8 absent), an altered form of SAGA, may be involved in positive transcriptional regulation. Besides lacking SPT8, SALSA contains an SPT7 subunit that is truncated. SLIK (SAGA-like) is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. TADA1, also called SPT3-associated factor 42, or STAF42, or transcriptional adapter 1-like protein (TADA1L), may be involved in transcriptional regulation. It functions as a component of the STAGA transcription coactivator-HAT complex, which is composed of at least SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP, and TAF9.

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gi 1958672853  63 QLEGRMIVTAYEHGL-DNVTEEAVSAVVYAVENHLKDILTSVvsrrkayrVRDGHFKYAFG 122
Cdd:cd22925     1 TLRTRMTGISYEHGLiGPVDDDVVDIMAIALENHLKGILEAA--------LTIEDFADALE 53

histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also called ADA1, is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TATA binding protein (TBP) interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA (SAGA altered, SPT8 absent), an altered form of SAGA, may be involved in positive transcriptional regulation. Besides lacking SPT8, SALSA contains an SPT7 subunit that is truncated. SLIK (SAGA-like) is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box.

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gi 1958672853  51 LCSHTMMLPTRGQLEGRMIVTAYEHGLD-NVTEEAVSAVVYAVENHLKDILTSVVSRRKAYR 111
Cdd:cd22933     1 LCSESKELPDADSLRERMTGIALENGLLgGVAEECVELLLLALEQHLKNILSSCIDKVRARR 62

histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.

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gi 1958672853  74 EHGLDNVTEEAVSAVVYAVENHLKDILTSVVS----RRKAYRVRdghFKYAFGSNVTPQ 128
Cdd:cd08045    20 KHGLKEVSPDVLSLLSLAVQERLRDLLEKLIVaskhRVDSEKPD---YRYEVTSDVRRQ 75