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Conserved domains on  [gi|15242340|ref|NP_197061|]
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Bromodomain transcription factor [Arabidopsis thaliana]

Protein Classification

TBP-associated factor 8 family protein( domain architecture ID 10651827)

TATA binding protein (TBP)-associated factor 8 (TAF8) family protein is one of several general cofactors which are typically involved in gene activation to bring about the communication between gene-specific transcription factors and components of the general transcription machinery

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTP smart00576
Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael ...
 25-116 1.89e-27

Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael histone-like transcription factors


:

Pssm-ID: 128846  Cd Length: 77  Bit Score: 103.56  E-value: 1.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340     25 NDFAYALARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIV 104
Cdd:smart00576   1 NELAFALLRIAVAQILESAG---------------FDSFQESALETLTDILQSYIQELGRTAHSYAELAGRTEPNLGDVV 65

                           90
                   ....*....|..
gi 15242340    105 QALEDLGSGLGF 116
Cdd:smart00576  66 LALENLGISVGE 77
TAF8 super family cl11065
TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated ...
 176-221 9.39e-04

TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated Factor 8 (TAF8) is one of several TAFs that bind TBP, and is involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and the assembly of the preinitiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions, such as serving as activator-binding sites, involvement in the core-promoter recognition, or a role in the essential catalytic activity of the complex. The mouse ortholog of TAF8 is called taube nuss protein (TBN), and is required for early embryonic development. TBN mutant mice exhibit disturbances in the balance between cell death and cell survival in the early embryo. TAF8 plays a role in the differentiation of preadipocyte fibroblasts to adipocytes; it is also required for the integration of TAF10 into the TAF complex. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF8 is also a component of a small TAF complex (SMAT), which contains TAF8, TAF10 and SUPT7L. Several TAFs interact via histone-fold motifs. The histone fold (HFD) is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. TAF8 contains an H4 related histone fold motif, and interacts with several subunits of TFIID, including TBP and the histone-fold protein TAF10. Currently, five HF-containing TAF pairs have been described or suggested to exist in TFIID: TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


The actual alignment was detected with superfamily member cd08049:

Pssm-ID: 448101  Cd Length: 54  Bit Score: 36.87  E-value: 9.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15242340 176 EHIPVWLPAFPE--------TKMSNGSEEInVDKIERDVQSRDNGSSLMSVQQS 221
Cdd:cd08049   1 AHIPSWLPPFPDphtykrtpTYSERETDPK-KLREELASQRRLAEKALLRLQQK 53
 
Name Accession Description Interval E-value
BTP smart00576
Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael ...
 25-116 1.89e-27

Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael histone-like transcription factors


Pssm-ID: 128846  Cd Length: 77  Bit Score: 103.56  E-value: 1.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340     25 NDFAYALARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIV 104
Cdd:smart00576   1 NELAFALLRIAVAQILESAG---------------FDSFQESALETLTDILQSYIQELGRTAHSYAELAGRTEPNLGDVV 65

                           90
                   ....*....|..
gi 15242340    105 QALEDLGSGLGF 116
Cdd:smart00576  66 LALENLGISVGE 77
Bromo_TP pfam07524
Bromodomain associated; This domain is predicted to bind DNA and is often found associated ...
 27-111 1.43e-13

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.


Pssm-ID: 400073  Cd Length: 77  Bit Score: 65.42  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340    27 FAYALARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQA 106
Cdd:pfam07524   3 LAHDLLKVAVSQILEHAG---------------FDSAEESALETLTDIAQSYIRELGEQAKSFAEHAGRSEPTLFDVVLT 67


                  ....*
gi 15242340   107 LEDLG 111
Cdd:pfam07524  68 LVEMG 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 31-108 6.56e-12

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.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 60.31  E-value: 6.56e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242340  31 LARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQALE 108
Cdd:cd00076   1 LLRSAVARILKSAG---------------FDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
TAF8 cd08049
TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated ...
 176-221 9.39e-04

TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated Factor 8 (TAF8) is one of several TAFs that bind TBP, and is involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and the assembly of the preinitiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions, such as serving as activator-binding sites, involvement in the core-promoter recognition, or a role in the essential catalytic activity of the complex. The mouse ortholog of TAF8 is called taube nuss protein (TBN), and is required for early embryonic development. TBN mutant mice exhibit disturbances in the balance between cell death and cell survival in the early embryo. TAF8 plays a role in the differentiation of preadipocyte fibroblasts to adipocytes; it is also required for the integration of TAF10 into the TAF complex. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF8 is also a component of a small TAF complex (SMAT), which contains TAF8, TAF10 and SUPT7L. Several TAFs interact via histone-fold motifs. The histone fold (HFD) is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. TAF8 contains an H4 related histone fold motif, and interacts with several subunits of TFIID, including TBP and the histone-fold protein TAF10. Currently, five HF-containing TAF pairs have been described or suggested to exist in TFIID: TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 176263  Cd Length: 54  Bit Score: 36.87  E-value: 9.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15242340 176 EHIPVWLPAFPE--------TKMSNGSEEInVDKIERDVQSRDNGSSLMSVQQS 221
Cdd:cd08049   1 AHIPSWLPPFPDphtykrtpTYSERETDPK-KLREELASQRRLAEKALLRLQQK 53
 
Name Accession Description Interval E-value
BTP smart00576
Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael ...
 25-116 1.89e-27

Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael histone-like transcription factors


Pssm-ID: 128846  Cd Length: 77  Bit Score: 103.56  E-value: 1.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340     25 NDFAYALARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIV 104
Cdd:smart00576   1 NELAFALLRIAVAQILESAG---------------FDSFQESALETLTDILQSYIQELGRTAHSYAELAGRTEPNLGDVV 65

                           90
                   ....*....|..
gi 15242340    105 QALEDLGSGLGF 116
Cdd:smart00576  66 LALENLGISVGE 77
Bromo_TP pfam07524
Bromodomain associated; This domain is predicted to bind DNA and is often found associated ...
 27-111 1.43e-13

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.


Pssm-ID: 400073  Cd Length: 77  Bit Score: 65.42  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340    27 FAYALARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQA 106
Cdd:pfam07524   3 LAHDLLKVAVSQILEHAG---------------FDSAEESALETLTDIAQSYIRELGEQAKSFAEHAGRSEPTLFDVVLT 67


                  ....*
gi 15242340   107 LEDLG 111
Cdd:pfam07524  68 LVEMG 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 31-108 6.56e-12

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.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 60.31  E-value: 6.56e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242340  31 LARMATAQICESVEinsyqessqsreglrFSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQALE 108
Cdd:cd00076   1 LLRSAVARILKSAG---------------FDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_TAF3 cd22916
histone-fold domain found in transcription initiation factor TFIID subunit 3 (TAF3) and ...
 27-111 1.39e-10

histone-fold domain found in transcription initiation factor TFIID subunit 3 (TAF3) and similar proteins; TAF3, also called TATA Binding Protein (TBP) associated factor 3, 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, or transcription initiation factor TFIID 140 kDa subunit (TAF(II)140, TAF140, TAFII-140,TAFII140), 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.


Pssm-ID: 467041  Cd Length: 92  Bit Score: 57.23  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340  27 FAYALARMATAQICESVEINSYQESsqsreglrfssfqetALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQA 106
Cdd:cd22916   3 FSRSLLRVVVAQICQNVGWHSIQSS---------------PLDLLTDVLQRYLLELARSAHRYAEQYGRTEPNLDDLGLA 67


                ....*
gi 15242340 107 LEDLG 111
Cdd:cd22916  68 FKDMG 72
HFD_TAF8 cd22918
histone-fold domain found in transcription initiation factor TFIID subunit 8 (TAF8) and ...
 60-111 3.45e-09

histone-fold domain found in transcription initiation factor TFIID subunit 8 (TAF8) and similar proteins; TAF8, also called TATA Binding Protein (TBP) associated factor 8, protein taube nuss, TBP-associated factor 43 kDa, TBP-associated factor 8, or transcription initiation factor TFIID 43 kDa subunit (TAFII-43, TAFII43), 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. TAF8 mediates both basal and activator-dependent transcription. It is involved in the differentiation of preadipocyte fibroblasts to adipocytes, however, it does not seem to play a role in differentiation of myoblasts. TAF8 is required for the integration of TAF10 in the TAF complex. It may be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo.


Pssm-ID: 467043  Cd Length: 84  Bit Score: 53.32  E-value: 3.45e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242340  60 FSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQALEDLG 111
Cdd:cd22918  19 FESAEKSALETLTEMLQSYLTEIGRSSKAYCELAGRTEPTLSDVVLALIDMG 70
HFD_SPT7 cd22927
histone-fold domain found in protein SPT7 and similar proteins; SPT7, also called suppressor ...
 60-145 4.08e-07

histone-fold domain found in protein SPT7 and similar proteins; SPT7, also called suppressor of Ty 7 homolog, 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. SPT7 is transcriptional activator of TY elements and other genes.


Pssm-ID: 467052  Cd Length: 117  Bit Score: 48.31  E-value: 4.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242340  60 FSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNALDIVQALEDLGSglgfDGAHDVEHCLADsgvvkDIIRYT 139
Cdd:cd22927  29 FEGAQPSALDVLTDIAADYLSNLGRTLRLYLDRYSKKMSPEEILLHTLFENGV----EDISDLESYIKD-----DVERYG 99


                ....*.
gi 15242340 140 GEAEEI 145
Cdd:cd22927 100 GKLSDL 105
HFD_SUPT7L cd06847
histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, ...
 60-113 3.33e-05

histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, also called STAGA complex 65 subunit gamma, adenocarcinoma antigen ART1, SPTF-associated factor 65 gamma, or STAF65gamma, is the ortholog of yeast SPT7 in mammalian cells. It is highly similar to yeast SPT7 but lacks the N-terminal SPT7 bromodomain. SUPT7L is a protein component specific to STAGA (SPT3-TAF9-GCN5 Acetyltransferase)-type complexes. It plays an essential role for the integrity of the STAGA complex.


Pssm-ID: 467022  Cd Length: 86  Bit Score: 41.78  E-value: 3.33e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242340  60 FSSFQETALETLTDVVIQYIQNIGKTAQFYVNMAGRVESNA-LDIV-QALEDLGSG 113
Cdd:cd06847  22 FDSASESALEVLTDVLDEFLRKFTRLLRSAVDREALSGETGfPDILeRVLHEMGIG 77
TAF8 cd08049
TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated ...
 176-221 9.39e-04

TATA Binding Protein (TBP) Associated Factor 8; The TATA Binding Protein (TBP) Associated Factor 8 (TAF8) is one of several TAFs that bind TBP, and is involved in forming the Transcription Factor IID (TFIID) complex. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) that are involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and the assembly of the preinitiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions, such as serving as activator-binding sites, involvement in the core-promoter recognition, or a role in the essential catalytic activity of the complex. The mouse ortholog of TAF8 is called taube nuss protein (TBN), and is required for early embryonic development. TBN mutant mice exhibit disturbances in the balance between cell death and cell survival in the early embryo. TAF8 plays a role in the differentiation of preadipocyte fibroblasts to adipocytes; it is also required for the integration of TAF10 into the TAF complex. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF8 is also a component of a small TAF complex (SMAT), which contains TAF8, TAF10 and SUPT7L. Several TAFs interact via histone-fold motifs. The histone fold (HFD) is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. TAF8 contains an H4 related histone fold motif, and interacts with several subunits of TFIID, including TBP and the histone-fold protein TAF10. Currently, five HF-containing TAF pairs have been described or suggested to exist in TFIID: TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 176263  Cd Length: 54  Bit Score: 36.87  E-value: 9.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15242340 176 EHIPVWLPAFPE--------TKMSNGSEEInVDKIERDVQSRDNGSSLMSVQQS 221
Cdd:cd08049   1 AHIPSWLPPFPDphtykrtpTYSERETDPK-KLREELASQRRLAEKALLRLQQK 53
 
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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