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Conserved domains on  [gi|6325001|ref|NP_015069|]
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Hfi1p [Saccharomyces cerevisiae S288C]

Protein Classification

TADA1 family protein( domain architecture ID 10579535)

TADA1 (transcriptional adapter 1) family protein similar to human TADA1 is a component of the STAGA transcription coactivator-HAT complex that may be involved in transcriptional regulation, and to Saccharomyces cerevisiae transcriptional coactivator HFI1/ADA1 that is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 60-316 1.40e-41

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.


:

Pssm-ID: 463692  Cd Length: 135  Bit Score: 144.93  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001     60 RIDLGAMIEELTSLLGKESWTKYAQIISLFILGKLSRKELSNELELVFSPSaasleksntnhhhsLVRLHNQLLLGIFAN 139
Cdd:pfam12767   1 RIDLEELKTQLKKKLGPERWEKYFEALSRFLSGKLSKAELDKLCDPILGRE--------------NLHLHNQLILSILAN 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    140 Slrenplgrngnesswgfgngsnnpnnklkrinkhnsqievykkivmslplndrnrlkmitkeagkrgfifcsvfqarln 219
Cdd:pfam12767  67 A------------------------------------------------------------------------------- 67

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    220 nipkipivtnpeslkrvksnnlktplewsQDIMNGFNVPLASESHSLPDTDSFYLRMVGIAREHGLVGTVDARCVELISL 299
Cdd:pfam12767  68 -----------------------------QEIRSPYAAPLAYESGELPDTDSLRKRMEPIAYEHGLVGGVSADCANLLNN 118

                         250
                  ....*....|....*..
gi 6325001    300 ALDQYLKNIIEFTIDTV 316
Cdd:pfam12767 119 ALDVYLKNLLESCIDLV 135
 
Name Accession Description Interval E-value
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 60-316 1.40e-41

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.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 144.93  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001     60 RIDLGAMIEELTSLLGKESWTKYAQIISLFILGKLSRKELSNELELVFSPSaasleksntnhhhsLVRLHNQLLLGIFAN 139
Cdd:pfam12767   1 RIDLEELKTQLKKKLGPERWEKYFEALSRFLSGKLSKAELDKLCDPILGRE--------------NLHLHNQLILSILAN 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    140 Slrenplgrngnesswgfgngsnnpnnklkrinkhnsqievykkivmslplndrnrlkmitkeagkrgfifcsvfqarln 219
Cdd:pfam12767  67 A------------------------------------------------------------------------------- 67

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    220 nipkipivtnpeslkrvksnnlktplewsQDIMNGFNVPLASESHSLPDTDSFYLRMVGIAREHGLVGTVDARCVELISL 299
Cdd:pfam12767  68 -----------------------------QEIRSPYAAPLAYESGELPDTDSLRKRMEPIAYEHGLVGGVSADCANLLNN 118

                         250
                  ....*....|....*..
gi 6325001    300 ALDQYLKNIIEFTIDTV 316
Cdd:pfam12767 119 ALDVYLKNLLESCIDLV 135
HFD_HFI1 cd22933
histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also ...
 259-320 1.58e-25

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.


Pssm-ID: 467057  Cd Length: 87  Bit Score: 99.60  E-value: 1.58e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325001  259 LASESHSLPDTDSFYLRMVGIAREHGLVGTVDARCVELISLALDQYLKNIIEFTIDTVRYRR 320
Cdd:cd22933   1 LCSESKELPDADSLRERMTGIALENGLLGGVAEECVELLLLALEQHLKNILSSCIDKVRARR 62
 
Name Accession Description Interval E-value
SAGA-Tad1 pfam12767
Transcriptional regulator of RNA polII, SAGA, subunit; The yeast SAGA complex is a ...
 60-316 1.40e-41

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.


Pssm-ID: 463692  Cd Length: 135  Bit Score: 144.93  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001     60 RIDLGAMIEELTSLLGKESWTKYAQIISLFILGKLSRKELSNELELVFSPSaasleksntnhhhsLVRLHNQLLLGIFAN 139
Cdd:pfam12767   1 RIDLEELKTQLKKKLGPERWEKYFEALSRFLSGKLSKAELDKLCDPILGRE--------------NLHLHNQLILSILAN 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    140 Slrenplgrngnesswgfgngsnnpnnklkrinkhnsqievykkivmslplndrnrlkmitkeagkrgfifcsvfqarln 219
Cdd:pfam12767  67 A------------------------------------------------------------------------------- 67

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325001    220 nipkipivtnpeslkrvksnnlktplewsQDIMNGFNVPLASESHSLPDTDSFYLRMVGIAREHGLVGTVDARCVELISL 299
Cdd:pfam12767  68 -----------------------------QEIRSPYAAPLAYESGELPDTDSLRKRMEPIAYEHGLVGGVSADCANLLNN 118

                         250
                  ....*....|....*..
gi 6325001    300 ALDQYLKNIIEFTIDTV 316
Cdd:pfam12767 119 ALDVYLKNLLESCIDLV 135
HFD_HFI1 cd22933
histone-fold domain found in transcriptional coactivator HFI1 and similar proteins; HFI1, also ...
 259-320 1.58e-25

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.


Pssm-ID: 467057  Cd Length: 87  Bit Score: 99.60  E-value: 1.58e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325001  259 LASESHSLPDTDSFYLRMVGIAREHGLVGTVDARCVELISLALDQYLKNIIEFTIDTVRYRR 320
Cdd:cd22933   1 LCSESKELPDADSLRERMTGIALENGLLGGVAEECVELLLLALEQHLKNILSSCIDKVRARR 62
HFD_HFI1-like cd22925
histone-fold domain found in transcriptional coactivator HFI1, transcriptional adapter 1 ...
 275-314 3.43e-08

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.


Pssm-ID: 467050  Cd Length: 53  Bit Score: 49.73  E-value: 3.43e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6325001  275 RMVGIAREHGLVGTVDARCVELISLALDQYLKNIIEFTID 314
Cdd:cd22925   5 RMTGISYEHGLIGPVDDDVVDIMAIALENHLKGILEAALT 44
HFD_TADA1 cd22934
histone-fold domain found in transcriptional adapter 1 (TADA1) and similar proteins; TADA1, ...
 266-324 1.84e-05

histone-fold domain found in transcriptional adapter 1 (TADA1) and similar proteins; 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 at least of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9.


Pssm-ID: 467058  Cd Length: 84  Bit Score: 42.93  E-value: 1.84e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6325001  266 LPDTDSFYLRMVGIAREHGLVGtVDARCVELISLALDQYLKNIIEFTIDtvryRRKKYS 324
Cdd:cd22934   1 LPDIAMLHGRMLVTAWECGLDG-VTDNAVELVVQAVENFLKNIITAVIS----RRKGYR 54
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
 275-321 6.97e-04

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 41.49  E-value: 6.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6325001    275 RMVGIAREHGLvGTVDARCVELISLALDQYLKNIIEFTIDTVRYRRK 321
Cdd:pfam05236  53 KILEIAKKNGL-KEIDPDVLELLSHACEERLRNLLEKLIVISRHRRD 98
HFD_TAF4 cd08045
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
 275-319 4.82e-03

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.


Pssm-ID: 467027 [Multi-domain]  Cd Length: 100  Bit Score: 36.44  E-value: 4.82e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6325001  275 RMVGIAREHGLvGTVDARCVELISLALDQYLKNIIEFTIDTVRYR 319
Cdd:cd08045  13 KIQKIAKKHGL-KEVSPDVLSLLSLAVQERLRDLLEKLIVASKHR 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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