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Conserved domains on  [gi|1207180330|ref|XP_021333225|]
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TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
99-311 1.18e-85

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


:

Pssm-ID: 381749  Cd Length: 216  Bit Score: 265.66  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330  99 LSEDLLKYYQQITRAILGEDPHLMKVALLDLQSNSKIAALLPYFVYVIS-GVKSVSHDLDQLNRLLHMVKSLVQNPYLYL 177
Cdd:cd08050     4 LSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAeGVTKNLRNLALLIYLLRMVRALLDNPHLFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 178 GSYVRSLVSSVMYCILEPLAASINPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAV 257
Cdd:cd08050    84 EPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTHYGAI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207180330 258 VGLHALGWKAVERVLYPHLPAYWANLQAVLDDySVSNAQVKADGHKVYGAILVA 311
Cdd:cd08050   164 VGLAALGPEAVRALLLPNLKAYLERLESELED-SSSNALKRIEAEKVYGALLKA 216
HFD_SF super family cl45933
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
1-28 1.73e-10

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.


The actual alignment was detected with superfamily member cd22932:

Pssm-ID: 480273  Cd Length: 72  Bit Score: 57.21  E-value: 1.73e-10
                          10        20
                  ....*....|....*....|....*...
gi 1207180330   1 MRHAKRRKLSVEDFNRALRWSNTETVCG 28
Cdd:cd22932    45 MRHSKRRKLTTEDVNRALKWSDVEPVYG 72
 
Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
99-311 1.18e-85

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


Pssm-ID: 381749  Cd Length: 216  Bit Score: 265.66  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330  99 LSEDLLKYYQQITRAILGEDPHLMKVALLDLQSNSKIAALLPYFVYVIS-GVKSVSHDLDQLNRLLHMVKSLVQNPYLYL 177
Cdd:cd08050     4 LSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAeGVTKNLRNLALLIYLLRMVRALLDNPHLFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 178 GSYVRSLVSSVMYCILEPLAASINPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAV 257
Cdd:cd08050    84 EPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTHYGAI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207180330 258 VGLHALGWKAVERVLYPHLPAYWANLQAVLDDySVSNAQVKADGHKVYGAILVA 311
Cdd:cd08050   164 VGLAALGPEAVRALLLPNLKAYLERLESELED-SSSNALKRIEAEKVYGALLKA 216
TAF6 COG5095
Transcription initiation factor TFIID, subunit TAF6 (also component of histone ...
1-317 2.05e-31

Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227426 [Multi-domain]  Cd Length: 450  Bit Score: 127.01  E-value: 2.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330   1 MRHAKRRKLSVEDFNRALRWSNTETVCGYGAQDALPFRPLKEG---ELFYVEDREI------------------------ 53
Cdd:COG5095    50 MVHSKRTVLTIDDISYALRSLNVEPLYGYDPSRPLQFSLVFRGlgqSVYYLDDEEVdfeeyinrplpkvprrvsiqshwl 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330  54 -------------NLVELALATNIPKGCAETMVRVHVSYLDGKGNLEPQGTV---PTAVQSLSEDLLKYYQQITRAILGE 117
Cdd:COG5095   130 aiegvqpaipqnpILLDKPVAKWASKDTLGVMPGASTAAYQARNGVTSMENAelkPLVKHVLSKELQMYFDKVISALLDE 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 118 -DPHLMKVALLDLQSNSKIAALLPYFVYVISG--VKSVShDLDQLNRLLHMVKSLVQNPYLYLGSYVRSLVSSVMYCILE 194
Cdd:COG5095   210 sDEQTRDAALESLRNDSGLHQLVPYFIHFFNEqiTKNLK-NLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMPSILTCLIA 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 195 PLAASINPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAVVGLHALGWKAVERVLYP 274
Cdd:COG5095   289 KKLGNVPDDHEHYALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGALKGLSILSKEVIRTVIKP 368
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1207180330 275 HLpAYWANLqaVLDDYSVSNAQVKADGHKVYGAILVAVERLLK 317
Cdd:COG5095   369 NA-DYYVRL--VNKTLEKGNEEEIYENNRVVDLLKDALLILQS 408
TAF6_C pfam07571
TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the ...
188-277 2.00e-25

TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9.


Pssm-ID: 462212  Cd Length: 90  Bit Score: 100.25  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 188 VMYCILeplAASI---NPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAVVGLHALG 264
Cdd:pfam07571   1 ILTCLV---AKKLgarPPLDDHWALRDFAASLLAQICRKYSSSYPTLKPRITRTLLKALLDPKKPLGTHYGALIGLAALG 77
                          90
                  ....*....|...
gi 1207180330 265 WKAVERVLYPHLP 277
Cdd:pfam07571  78 PEAIRALILPNLK 90
HFD_TAF6L cd22932
histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated ...
1-28 1.73e-10

histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) and similar proteins; TAF6L, also called PCAF-associated factor 65-alpha (PAF65-alpha), is a component of the PCAF complex, which can efficiently acetylate histones in a nucleosomal context. The PCAF complex is composed of several TBP-associated factors (TAFs) and PCAF-associated factors (PAFs). It might be the human version of the yeast SAGA complex. With TAF5L, TAF6L acts as an epigenetic regulator essential for somatic reprogramming. It also regulates target genes through H3K9ac deposition and MYC recruitment, which trigger the MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.


Pssm-ID: 467056  Cd Length: 72  Bit Score: 57.21  E-value: 1.73e-10
                          10        20
                  ....*....|....*....|....*...
gi 1207180330   1 MRHAKRRKLSVEDFNRALRWSNTETVCG 28
Cdd:cd22932    45 MRHSKRRKLTTEDVNRALKWSDVEPVYG 72
TAF smart00803
TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) ...
1-19 7.60e-05

TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) are part of the transcription initiation factor TFIID multimeric protein complex. TFIID is composed of the TATA box binding protein (TBP) and a number of TAFs. The TAFs provide binding sites for many different transcriptional activators and co-activators that modulate transcription initiation by Pol II. TAF proteins adopt a histone-like fold.


Pssm-ID: 129039  Cd Length: 65  Bit Score: 41.07  E-value: 7.60e-05
                           10
                   ....*....|....*....
gi 1207180330    1 MRHAKRRKLSVEDFNRALR 19
Cdd:smart00803  47 MRHSKRTTLTTSDIDSALR 65
TAF pfam02969
TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.
1-19 4.57e-04

TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.


Pssm-ID: 427084  Cd Length: 66  Bit Score: 38.57  E-value: 4.57e-04
                          10
                  ....*....|....*....
gi 1207180330   1 MRHAKRRKLSVEDFNRALR 19
Cdd:pfam02969  48 MRHSKRTKLTVADVDSALR 66
 
Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
99-311 1.18e-85

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


Pssm-ID: 381749  Cd Length: 216  Bit Score: 265.66  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330  99 LSEDLLKYYQQITRAILGEDPHLMKVALLDLQSNSKIAALLPYFVYVIS-GVKSVSHDLDQLNRLLHMVKSLVQNPYLYL 177
Cdd:cd08050     4 LSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAeGVTKNLRNLALLIYLLRMVRALLDNPHLFL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 178 GSYVRSLVSSVMYCILEPLAASINPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAV 257
Cdd:cd08050    84 EPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTHYGAI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207180330 258 VGLHALGWKAVERVLYPHLPAYWANLQAVLDDySVSNAQVKADGHKVYGAILVA 311
Cdd:cd08050   164 VGLAALGPEAVRALLLPNLKAYLERLESELED-SSSNALKRIEAEKVYGALLKA 216
TAF6 COG5095
Transcription initiation factor TFIID, subunit TAF6 (also component of histone ...
1-317 2.05e-31

Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227426 [Multi-domain]  Cd Length: 450  Bit Score: 127.01  E-value: 2.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330   1 MRHAKRRKLSVEDFNRALRWSNTETVCGYGAQDALPFRPLKEG---ELFYVEDREI------------------------ 53
Cdd:COG5095    50 MVHSKRTVLTIDDISYALRSLNVEPLYGYDPSRPLQFSLVFRGlgqSVYYLDDEEVdfeeyinrplpkvprrvsiqshwl 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330  54 -------------NLVELALATNIPKGCAETMVRVHVSYLDGKGNLEPQGTV---PTAVQSLSEDLLKYYQQITRAILGE 117
Cdd:COG5095   130 aiegvqpaipqnpILLDKPVAKWASKDTLGVMPGASTAAYQARNGVTSMENAelkPLVKHVLSKELQMYFDKVISALLDE 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 118 -DPHLMKVALLDLQSNSKIAALLPYFVYVISG--VKSVShDLDQLNRLLHMVKSLVQNPYLYLGSYVRSLVSSVMYCILE 194
Cdd:COG5095   210 sDEQTRDAALESLRNDSGLHQLVPYFIHFFNEqiTKNLK-NLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMPSILTCLIA 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 195 PLAASINPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAVVGLHALGWKAVERVLYP 274
Cdd:COG5095   289 KKLGNVPDDHEHYALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGALKGLSILSKEVIRTVIKP 368
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1207180330 275 HLpAYWANLqaVLDDYSVSNAQVKADGHKVYGAILVAVERLLK 317
Cdd:COG5095   369 NA-DYYVRL--VNKTLEKGNEEEIYENNRVVDLLKDALLILQS 408
TAF6_C pfam07571
TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the ...
188-277 2.00e-25

TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9.


Pssm-ID: 462212  Cd Length: 90  Bit Score: 100.25  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207180330 188 VMYCILeplAASI---NPLNDHWTLRDYAALLLSHIFWTHGDLVSGLYHQILLSLQKVLSDPVRPLCSHYGAVVGLHALG 264
Cdd:pfam07571   1 ILTCLV---AKKLgarPPLDDHWALRDFAASLLAQICRKYSSSYPTLKPRITRTLLKALLDPKKPLGTHYGALIGLAALG 77
                          90
                  ....*....|...
gi 1207180330 265 WKAVERVLYPHLP 277
Cdd:pfam07571  78 PEAIRALILPNLK 90
HFD_TAF6L cd22932
histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated ...
1-28 1.73e-10

histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) and similar proteins; TAF6L, also called PCAF-associated factor 65-alpha (PAF65-alpha), is a component of the PCAF complex, which can efficiently acetylate histones in a nucleosomal context. The PCAF complex is composed of several TBP-associated factors (TAFs) and PCAF-associated factors (PAFs). It might be the human version of the yeast SAGA complex. With TAF5L, TAF6L acts as an epigenetic regulator essential for somatic reprogramming. It also regulates target genes through H3K9ac deposition and MYC recruitment, which trigger the MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.


Pssm-ID: 467056  Cd Length: 72  Bit Score: 57.21  E-value: 1.73e-10
                          10        20
                  ....*....|....*....|....*...
gi 1207180330   1 MRHAKRRKLSVEDFNRALRWSNTETVCG 28
Cdd:cd22932    45 MRHSKRRKLTTEDVNRALKWSDVEPVYG 72
TAF smart00803
TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) ...
1-19 7.60e-05

TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) are part of the transcription initiation factor TFIID multimeric protein complex. TFIID is composed of the TATA box binding protein (TBP) and a number of TAFs. The TAFs provide binding sites for many different transcriptional activators and co-activators that modulate transcription initiation by Pol II. TAF proteins adopt a histone-like fold.


Pssm-ID: 129039  Cd Length: 65  Bit Score: 41.07  E-value: 7.60e-05
                           10
                   ....*....|....*....
gi 1207180330    1 MRHAKRRKLSVEDFNRALR 19
Cdd:smart00803  47 MRHSKRTTLTTSDIDSALR 65
HFD_TAF6 cd22931
histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and ...
1-19 1.25e-04

histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and similar proteins; TAF6, also called TATA Binding Protein (TBP) associated factor 6, RNA polymerase II TBP-associated factor subunit E, transcription initiation factor TFIID 70 kDa subunit (TAF(II)70, TAFII-70, TAFII70), or transcription initiation factor TFIID 80 kDa subunit (TAF(II)80, TAFII-80, TAFII80), is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC.


Pssm-ID: 467055  Cd Length: 66  Bit Score: 40.17  E-value: 1.25e-04
                          10
                  ....*....|....*....
gi 1207180330   1 MRHAKRRKLSVEDFNRALR 19
Cdd:cd22931    47 MRHSKRTKLTTDDIDNALR 65
TAF pfam02969
TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.
1-19 4.57e-04

TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.


Pssm-ID: 427084  Cd Length: 66  Bit Score: 38.57  E-value: 4.57e-04
                          10
                  ....*....|....*....
gi 1207180330   1 MRHAKRRKLSVEDFNRALR 19
Cdd:pfam02969  48 MRHSKRTKLTVADVDSALR 66
HFD_TAF6-like cd22917
histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and ...
1-20 5.99e-03

histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and similar proteins; This subfamily includes TAF6 and TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L). TAF6, also called TATA Binding Protein (TBP) associated factor 6, RNA polymerase II TBP-associated factor subunit E, transcription initiation factor TFIID 70 kDa subunit (TAF(II)70, TAFII-70, TAFII70), or transcription initiation factor TFIID 80 kDa subunit, (TAF(II)80, TAFII-80, TAFII80), is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAF6L, also called PCAF-associated factor 65-alpha (PAF65-alpha), is a component of the PCAF complex, which can efficiently acetylate histones in a nucleosomal context. The PCAF complex is composed of several TAFs and PCAF-associated factors (PAFs). It might be the human version of the yeast SAGA complex. With TAF5L, TAF6L acts as an epigenetic regulator essential for somatic reprogramming. It also regulates target genes through H3K9ac deposition and MYC recruitment, which trigger the MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.


Pssm-ID: 467042  Cd Length: 64  Bit Score: 35.65  E-value: 5.99e-03
                          10        20
                  ....*....|....*....|
gi 1207180330   1 MRHAKRRKLSVEDFNRALRW 20
Cdd:cd22917    45 AHHSKRKKLTADDINNALRL 64
 
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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