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Conserved domains on  [gi|68299787|ref|NP_908937|]
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transcription initiation factor TFIID subunit 9 [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

Gene Ontology:  GO:0006352|GO:0003677|GO:0140297|GO:0005669|GO:0016251|GO:0046982
PubMed:  8598927|16858867

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 ...
 9-130 1.42e-75

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: 225.47  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787     9 PKSMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPP 88
Cdd:pfam02291   1 SKKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 68299787    89 RDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLK 130
Cdd:pfam02291  81 REFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
 
Name Accession Description Interval E-value
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
 9-130 1.42e-75

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: 225.47  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787     9 PKSMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPP 88
Cdd:pfam02291   1 SKKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 68299787    89 RDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLK 130
Cdd:pfam02291  81 REFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
HFD_TAF9 cd07979
histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and ...
 13-107 5.56e-53

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: 167.02  E-value: 5.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787  13 PKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPRDFL 92
Cdd:cd07979   1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRADHSFTQPPPRELL 80

                        90
                ....*....|....*
gi 68299787  93 LDIARQRNQTPLPLI 107
Cdd:cd07979  81 LELAAEKNSIPLPPI 95
TAF9 COG5094
Transcription initiation factor TFIID, subunit TAF9 (also component of histone ...
 6-135 3.49e-37

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


Pssm-ID: 227425  Cd Length: 145  Bit Score: 128.18  E-value: 3.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787   6 MASPK------SMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKK---PTVDADDVRLAIQ 76
Cdd:COG5094   1 MASGGlnlasvSGPRDVRLIHLILRSLGIEEYEPKVPLQLLEFAHRYTQDVLEDALVYAKHTGRghiATLGVEDVRLALA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 68299787  77 CRADQSFTSPPPRDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLKSLQKK 135
Cdd:COG5094  81 TKVGRHFVPPPPKEYLLELATERNSKPLPQPDGENGIRLPPEKYCLTNLDWEVLRKDPK 139
 
Name Accession Description Interval E-value
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
 9-130 1.42e-75

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: 225.47  E-value: 1.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787     9 PKSMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPP 88
Cdd:pfam02291   1 SKKRPRDARLIHLILASMGITEYEPRVPLQLLEFAYRYTTDVLEDALVYSEHAGKKQIDVDDVRLAIQSRVNHQFTGPPP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 68299787    89 RDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLK 130
Cdd:pfam02291  81 REFLLELARERNSKPLPPVKPHYGLRLPPERYCLTAPNYDLK 122
HFD_TAF9 cd07979
histone-fold domain found in transcription initiation factor TFIID subunit 9 (TAF9) and ...
 13-107 5.56e-53

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: 167.02  E-value: 5.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787  13 PKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQCRADQSFTSPPPRDFL 92
Cdd:cd07979   1 PRDAQVIRAILKSMGVTDYEPRVVNQLLEFAYRYTTEVLQDAKVYAEHAGRSQIDEEDVRLAIQSRADHSFTQPPPRELL 80

                        90
                ....*....|....*
gi 68299787  93 LDIARQRNQTPLPLI 107
Cdd:cd07979  81 LELAAEKNSIPLPPI 95
TAF9 COG5094
Transcription initiation factor TFIID, subunit TAF9 (also component of histone ...
 6-135 3.49e-37

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


Pssm-ID: 227425  Cd Length: 145  Bit Score: 128.18  E-value: 3.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787   6 MASPK------SMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKK---PTVDADDVRLAIQ 76
Cdd:COG5094   1 MASGGlnlasvSGPRDVRLIHLILRSLGIEEYEPKVPLQLLEFAHRYTQDVLEDALVYAKHTGRghiATLGVEDVRLALA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 68299787  77 CRADQSFTSPPPRDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLKSLQKK 135
Cdd:COG5094  81 TKVGRHFVPPPPKEYLLELATERNSKPLPQPDGENGIRLPPEKYCLTNLDWEVLRKDPK 139
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 17-76 2.41e-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: 49.52  E-value: 2.41e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68299787  17 QMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRLAIQ 76
Cdd:cd00076   4 SAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 30-73 1.88e-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: 39.09  E-value: 1.88e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 68299787  30 EYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRL 73
Cdd:cd22919  23 TVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKL 66
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 20-73 9.80e-03

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 464782  Cd Length: 76  Bit Score: 34.09  E-value: 9.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 68299787    20 AQILKDMGI---TEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKPTVDADDVRL 73
Cdd:pfam15630  12 GKIVEEETLdlgVNATPQFIAALTELVYKQLENLAKDLEAFAKHAGRSTITTDDVKL 68
 
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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