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Conserved domains on  [gi|2462610257|ref|XP_054212243|]
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transcription initiation factor TFIID subunit 11 isoform X1 [Homo sapiens]

Protein Classification

transcription initiation factor TFIID subunit 11 family protein( domain architecture ID 10520364)

transcription initiation factor TFIID subunit 11 (TAF11) family protein family protein similar to Drosophila melanogaster transcription initiation factor TFIID subunit 11 (TAF11), a component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription

CATH:  1.10.20.10
Gene Ontology:  GO:0046982|GO:0051123|GO:0005669
PubMed:  31751889|14969724|19308322
SCOP:  4000797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TAFII28 pfam04719
hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of ...
 64-149 2.04e-54

hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. The conserved region is found at the C-terminal of most member proteins. The crystal structure of hTAFII28 with hTAFII18 shows that this region is involved in the binding of these two subunits. The conserved region contains four alpha helices and three loops arranged as in histone H3.


:

Pssm-ID: 428086  Cd Length: 86  Bit Score: 166.51  E-value: 2.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  64 ILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHM 143
Cdd:pfam04719   1 LLLSNFSEEQLDRYEVFRRSSFNKAVIKKLINSVLGQSVSQNVAIAVAGIAKVFVGEIVEEARDVQEEWGESGPLQPKHI 80


                  ....*.
gi 2462610257 144 REAVRR 149
Cdd:pfam04719  81 REAYRR 86
 
Name Accession Description Interval E-value
TAFII28 pfam04719
hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of ...
 64-149 2.04e-54

hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. The conserved region is found at the C-terminal of most member proteins. The crystal structure of hTAFII28 with hTAFII18 shows that this region is involved in the binding of these two subunits. The conserved region contains four alpha helices and three loops arranged as in histone H3.


Pssm-ID: 428086  Cd Length: 86  Bit Score: 166.51  E-value: 2.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  64 ILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHM 143
Cdd:pfam04719   1 LLLSNFSEEQLDRYEVFRRSSFNKAVIKKLINSVLGQSVSQNVAIAVAGIAKVFVGEIVEEARDVQEEWGESGPLQPKHI 80


                  ....*.
gi 2462610257 144 REAVRR 149
Cdd:pfam04719  81 REAYRR 86
HFD_TAF11 cd08048
histone-fold domain found in transcription initiation factor TFIID subunit 11 (TAF11) and ...
 69-154 2.66e-50

histone-fold domain found in transcription initiation factor TFIID subunit 11 (TAF11) and similar proteins; TAF11, also called TATA Binding Protein (TBP) associated factor 11, TFIID subunit p30-beta, or transcription initiation factor TFIID 28 kDa subunit (TAF(II)28, TAFII-28, TAFII28), 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. TAF11 interacts with the ligand binding domains of the nuclear receptors for vitamin D3 and thyroid hormone. TAF11 also directly interacts with TFIIA, acting as a bridging factor that stabilizes the TFIIA-TBP-DNA complex.


Pssm-ID: 467028  Cd Length: 87  Bit Score: 156.17  E-value: 2.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  69 FSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGE-MPPLQPKHMREAV 147
Cdd:cd08048     1 FTEEQLERYEAFRRSKFNKSAIKRLMQSVLGQSVSQNVVIVMAGIAKVFVGELVETARDVQEEWGEaTGPLQPKHLREAY 80


                  ....*..
gi 2462610257 148 RRLKSKG 154
Cdd:cd08048    81 RRLKAEG 87
TAF40 COG5251
Transcription initiation factor TFIID, subunit TAF11 [Transcription];
10-165 4.20e-32

Transcription initiation factor TFIID, subunit TAF11 [Transcription];


Pssm-ID: 227576  Cd Length: 199  Bit Score: 113.60  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  10 LKNKLESQDVSDLTTverEDSSllnpaakklKIDTKEKKekkqkvDEDEI---QKMQILVSSFSEEQLNRYEMYRRSAFP 86
Cdd:COG5251    56 PENDIEPDDILQQQT---QNSN---------YEDTNPGE------DENELaqdERFKLLVTNLDEEQTNRYEVFRRTSLN 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462610257  87 KAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKgqIPNSKHKKII 165
Cdd:COG5251   118 KTQVKKLASTVANQTVSPNIRIFLQGVGKVFVGEIIELAMIVQNKWLTSGPLIPFHKREAYRYKLKK--YLKKLTFSII 194
 
Name Accession Description Interval E-value
TAFII28 pfam04719
hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of ...
 64-149 2.04e-54

hTAFII28-like protein conserved region; The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. The conserved region is found at the C-terminal of most member proteins. The crystal structure of hTAFII28 with hTAFII18 shows that this region is involved in the binding of these two subunits. The conserved region contains four alpha helices and three loops arranged as in histone H3.


Pssm-ID: 428086  Cd Length: 86  Bit Score: 166.51  E-value: 2.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  64 ILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHM 143
Cdd:pfam04719   1 LLLSNFSEEQLDRYEVFRRSSFNKAVIKKLINSVLGQSVSQNVAIAVAGIAKVFVGEIVEEARDVQEEWGESGPLQPKHI 80


                  ....*.
gi 2462610257 144 REAVRR 149
Cdd:pfam04719  81 REAYRR 86
HFD_TAF11 cd08048
histone-fold domain found in transcription initiation factor TFIID subunit 11 (TAF11) and ...
 69-154 2.66e-50

histone-fold domain found in transcription initiation factor TFIID subunit 11 (TAF11) and similar proteins; TAF11, also called TATA Binding Protein (TBP) associated factor 11, TFIID subunit p30-beta, or transcription initiation factor TFIID 28 kDa subunit (TAF(II)28, TAFII-28, TAFII28), 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. TAF11 interacts with the ligand binding domains of the nuclear receptors for vitamin D3 and thyroid hormone. TAF11 also directly interacts with TFIIA, acting as a bridging factor that stabilizes the TFIIA-TBP-DNA complex.


Pssm-ID: 467028  Cd Length: 87  Bit Score: 156.17  E-value: 2.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  69 FSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGE-MPPLQPKHMREAV 147
Cdd:cd08048     1 FTEEQLERYEAFRRSKFNKSAIKRLMQSVLGQSVSQNVVIVMAGIAKVFVGELVETARDVQEEWGEaTGPLQPKHLREAY 80


                  ....*..
gi 2462610257 148 RRLKSKG 154
Cdd:cd08048    81 RRLKAEG 87
TAF40 COG5251
Transcription initiation factor TFIID, subunit TAF11 [Transcription];
10-165 4.20e-32

Transcription initiation factor TFIID, subunit TAF11 [Transcription];


Pssm-ID: 227576  Cd Length: 199  Bit Score: 113.60  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610257  10 LKNKLESQDVSDLTTverEDSSllnpaakklKIDTKEKKekkqkvDEDEI---QKMQILVSSFSEEQLNRYEMYRRSAFP 86
Cdd:COG5251    56 PENDIEPDDILQQQT---QNSN---------YEDTNPGE------DENELaqdERFKLLVTNLDEEQTNRYEVFRRTSLN 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462610257  87 KAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKgqIPNSKHKKII 165
Cdd:COG5251   118 KTQVKKLASTVANQTVSPNIRIFLQGVGKVFVGEIIELAMIVQNKWLTSGPLIPFHKREAYRYKLKK--YLKKLTFSII 194
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 85-148 5.24e-04

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: 36.43  E-value: 5.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462610257  85 FPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPlQPKHMREAVR 148
Cdd:cd00076     1 LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTP-NAEDVELALE 63
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 85-147 3.20e-03

Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes archaebacterial histones and histone like transcription factors from eukaryotes.


Pssm-ID: 395650  Cd Length: 65  Bit Score: 34.51  E-value: 3.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462610257  85 FPKAAIKRLIQSITGTS-VSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEmPPLQPKHMREAV 147
Cdd:pfam00808   3 LPIARVKRIMKSDPDAGrISQDAKELIAECVEEFIEFVASEAAEICNKAGR-KTINPEHIKQAV 65
 
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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