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Conserved domains on  [gi|6325246|ref|NP_015314|]
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Taf3p [Saccharomyces cerevisiae S288C]

Protein Classification

TBP-associated factor 9 domain-containing protein; TBP-associated factor 8 family protein( domain architecture ID 10651820)

TBP-associated factor 9 (TAF9) domain-containing protein is one of several TAFs with the histone fold motif that bind TBP and are involved in forming both histone acetyltransferase complex (SAGA) and TFIID complexes.| 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 ...
 5-83 2.30e-19

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


:

Pssm-ID: 128846  Cd Length: 77  Bit Score: 81.22  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325246       5 NDFYFALLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIA--QARCDQDdtiaLQDITLALENLGIVKP 82
Cdd:smart00576   1 NELAFALLRIAVAQILESAGFDSFQESALETLTDILQSYIQELGRTAHSYAelAGRTEPN----LGDVVLALENLGISVG 76


                   .
gi 6325246      83 T 83
Cdd:smart00576  77 E 77
 
Name Accession Description Interval E-value
BTP smart00576
Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael ...
 5-83 2.30e-19

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


Pssm-ID: 128846  Cd Length: 77  Bit Score: 81.22  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325246       5 NDFYFALLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIA--QARCDQDdtiaLQDITLALENLGIVKP 82
Cdd:smart00576   1 NELAFALLRIAVAQILESAGFDSFQESALETLTDILQSYIQELGRTAHSYAelAGRTEPN----LGDVVLALENLGISVG 76


                   .
gi 6325246      83 T 83
Cdd:smart00576  77 E 77
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 11-75 7.33e-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.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 54.53  E-value: 7.33e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325246   11 LLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIAQARCDQddTIALQDITLALE 75
Cdd:cd00076   1 LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRT--TPNAEDVELALE 63
 
Name Accession Description Interval E-value
BTP smart00576
Bromodomain transcription factors and PHD domain containing proteins; subdomain of archael ...
 5-83 2.30e-19

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


Pssm-ID: 128846  Cd Length: 77  Bit Score: 81.22  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325246       5 NDFYFALLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIA--QARCDQDdtiaLQDITLALENLGIVKP 82
Cdd:smart00576   1 NELAFALLRIAVAQILESAGFDSFQESALETLTDILQSYIQELGRTAHSYAelAGRTEPN----LGDVVLALENLGISVG 76


                   .
gi 6325246      83 T 83
Cdd:smart00576  77 E 77
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 11-75 7.33e-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.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 54.53  E-value: 7.33e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325246   11 LLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIAQARCDQddTIALQDITLALE 75
Cdd:cd00076   1 LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRT--TPNAEDVELALE 63
 
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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