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Conserved domains on  [gi|1937369648|ref|NP_598299|]
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transcription initiation factor TFIID subunit 9B [Rattus norvegicus]

Protein Classification

transcription initiation factor TFIID subunit 9 family protein( domain architecture ID 11130032)

transcription initiation factor TFIID subunit 9 family protein similar to Homo sapiens transcription initiation factor TFIID subunit 9 (TAF9), which is a component of the TFIID basal transcription factor complex that plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
5-125 2.88e-73

Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.


:

Pssm-ID: 460525  Cd Length: 122  Bit Score: 218.92  E-value: 2.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   5 KNAPRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPR 84
Cdd:pfam02291   2 KKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPPR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1937369648  85 DFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRLK 125
Cdd:pfam02291  82 EFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
 
Name Accession Description Interval E-value
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
5-125 2.88e-73

Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.


Pssm-ID: 460525  Cd Length: 122  Bit Score: 218.92  E-value: 2.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   5 KNAPRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPR 84
Cdd:pfam02291   2 KKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPPR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1937369648  85 DFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRLK 125
Cdd:pfam02291  82 EFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
HFD_TAF9 cd07979
histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and ...
8-102 1.54e-52

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.


Pssm-ID: 467024  Cd Length: 95  Bit Score: 165.47  E-value: 1.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   8 PRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPRDFL 87
Cdd:cd07979     1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRADHSFTQPPPRELL 80
                          90
                  ....*....|....*
gi 1937369648  88 LDIARQKNQTPLPLI 102
Cdd:cd07979    81 LELAAEKNSIPLPPI 95
TAF9 COG5094
Transcription initiation factor TFIID, subunit TAF9 (also component of histone ...
8-124 3.62e-35

Transcription initiation factor TFIID, subunit TAF9 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227425  Cd Length: 145  Bit Score: 122.78  E-value: 3.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   8 PRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKK---PTVDADDVRLAIQCRADQSFTSPPPR 84
Cdd:COG5094    14 PRDVRLIHLILRSLGIEEYEPKVPLQLLEFAHRYTQDVLEDALVYAKHTGRghiATLGVEDVRLALATKVGRHFVPPPPK 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937369648  85 DFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRL 124
Cdd:COG5094    94 EYLLELATERNSKPLPQPDGENGIRLPPEKYCLTNLDWEV 133
 
Name Accession Description Interval E-value
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
5-125 2.88e-73

Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.


Pssm-ID: 460525  Cd Length: 122  Bit Score: 218.92  E-value: 2.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   5 KNAPRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPR 84
Cdd:pfam02291   2 KKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPPR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1937369648  85 DFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRLK 125
Cdd:pfam02291  82 EFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
HFD_TAF9 cd07979
histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and ...
8-102 1.54e-52

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.


Pssm-ID: 467024  Cd Length: 95  Bit Score: 165.47  E-value: 1.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   8 PRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPRDFL 87
Cdd:cd07979     1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRADHSFTQPPPRELL 80
                          90
                  ....*....|....*
gi 1937369648  88 LDIARQKNQTPLPLI 102
Cdd:cd07979    81 LELAAEKNSIPLPPI 95
TAF9 COG5094
Transcription initiation factor TFIID, subunit TAF9 (also component of histone ...
8-124 3.62e-35

Transcription initiation factor TFIID, subunit TAF9 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227425  Cd Length: 145  Bit Score: 122.78  E-value: 3.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648   8 PRDALVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKK---PTVDADDVRLAIQCRADQSFTSPPPR 84
Cdd:COG5094    14 PRDVRLIHLILRSLGIEEYEPKVPLQLLEFAHRYTQDVLEDALVYAKHTGRghiATLGVEDVRLALATKVGRHFVPPPPK 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937369648  85 DFLLDIARQKNQTPLPLIKPYAGPRLPPDRYCLTAPNYRL 124
Cdd:COG5094    94 EYLLELATERNSKPLPQPDGENGIRLPPEKYCLTNLDWEV 133
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
13-71 2.98e-08

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: 49.14  E-value: 2.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369648  13 VMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQ 71
Cdd:cd00076     5 AVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
26-68 3.42e-04

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 38.31  E-value: 3.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1937369648  26 YEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRL 68
Cdd:cd22919    24 VSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKL 66
Bromo_TP pfam07524
Bromodomain associated; This domain is predicted to bind DNA and is often found associated ...
12-71 7.74e-03

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: 34.61  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369648  12 LVMAQILKDMGITDYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQ 71
Cdd:pfam07524  10 VAVSQILEHAGFDSAEESALETLTDIAQSYIRELGEQAKSFAEHAGRSEPTLFDVVLTLV 69
 
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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