NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30520009|ref|NP_848767|]
View 

transcription initiation protein SPT3 homolog [Mus musculus]

Protein Classification

TAF13 domain-containing protein( domain architecture ID 11129978)

TAF13 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TFIID-18kDa pfam02269
Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast ...
24-116 5.84e-39

Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast transcription factors and the 18kD subunit from human transcription initiation factor IID (TFIID-18). Determination of the crystal structure reveals an atypical histone fold


:

Pssm-ID: 190265  Cd Length: 93  Bit Score: 134.09  E-value: 5.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520009    24 ISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYMFI 103
Cdd:pfam02269   1 HLFRKELQSMMYGFGDVQDPLQETVQLLEDLVRGQLIELLQQAMKTAQLRGSRKITLEDIKFLIRKDPKKLNRLKDLLSM 80
                          90
                  ....*....|...
gi 30520009   104 RDYKSKIIKGIDE 116
Cdd:pfam02269  81 NELLKKARKQFDE 93
 
Name Accession Description Interval E-value
TFIID-18kDa pfam02269
Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast ...
24-116 5.84e-39

Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast transcription factors and the 18kD subunit from human transcription initiation factor IID (TFIID-18). Determination of the crystal structure reveals an atypical histone fold


Pssm-ID: 190265  Cd Length: 93  Bit Score: 134.09  E-value: 5.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520009    24 ISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYMFI 103
Cdd:pfam02269   1 HLFRKELQSMMYGFGDVQDPLQETVQLLEDLVRGQLIELLQQAMKTAQLRGSRKITLEDIKFLIRKDPKKLNRLKDLLSM 80
                          90
                  ....*....|...
gi 30520009   104 RDYKSKIIKGIDE 116
Cdd:pfam02269  81 NELLKKARKQFDE 93
HFD_TAF13 cd07978
histone-fold domain found in transcription initiation factor TFIID subunit 13 (TAF13) and ...
25-101 2.17e-33

histone-fold domain found in transcription initiation factor TFIID subunit 13 (TAF13) and similar proteins; TAF13, also called TATA Binding Protein (TBP) associated factor 13, transcription initiation factor TFIID 18 kDa subunit, TAF(II)18, TAFII-18, or TAFII18, is a component of the DNA-binding general RNA polymerase II transcription factor IID (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. TAF13 interacts with TBP, and more strongly with TAF10 and TAF11.


Pssm-ID: 467023  Cd Length: 77  Bit Score: 119.10  E-value: 2.17e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520009  25 SFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYM 101
Cdd:cd07978   1 LFTKEIRQMMYGFGDVRNPLPETVDLLEEIVIEYITDLLHKAMEVAKLRGSKKISVEDILFLLRKDPKKLARVKELL 77
TAF19 COG5248
Transcription initiation factor TFIID, subunit TAF13 [Transcription];
18-96 1.39e-08

Transcription initiation factor TFIID, subunit TAF13 [Transcription];


Pssm-ID: 227573  Cd Length: 126  Bit Score: 52.66  E-value: 1.39e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520009  18 RNAGKTISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGArvISAEDLLFLMRKDKKKLRR 96
Cdd:COG5248   3 REARRVNLFMKDIKSLMYAYGDVVAPRYDTAEALHEYVLDYMSILCTNAHNMAQVRNK--TKTEDFKFALRRDPKKLGR 79
 
Name Accession Description Interval E-value
TFIID-18kDa pfam02269
Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast ...
24-116 5.84e-39

Transcription initiation factor IID, 18kD subunit; This family includes the Spt3 yeast transcription factors and the 18kD subunit from human transcription initiation factor IID (TFIID-18). Determination of the crystal structure reveals an atypical histone fold


Pssm-ID: 190265  Cd Length: 93  Bit Score: 134.09  E-value: 5.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520009    24 ISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYMFI 103
Cdd:pfam02269   1 HLFRKELQSMMYGFGDVQDPLQETVQLLEDLVRGQLIELLQQAMKTAQLRGSRKITLEDIKFLIRKDPKKLNRLKDLLSM 80
                          90
                  ....*....|...
gi 30520009   104 RDYKSKIIKGIDE 116
Cdd:pfam02269  81 NELLKKARKQFDE 93
HFD_TAF13 cd07978
histone-fold domain found in transcription initiation factor TFIID subunit 13 (TAF13) and ...
25-101 2.17e-33

histone-fold domain found in transcription initiation factor TFIID subunit 13 (TAF13) and similar proteins; TAF13, also called TATA Binding Protein (TBP) associated factor 13, transcription initiation factor TFIID 18 kDa subunit, TAF(II)18, TAFII-18, or TAFII18, is a component of the DNA-binding general RNA polymerase II transcription factor IID (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. TAF13 interacts with TBP, and more strongly with TAF10 and TAF11.


Pssm-ID: 467023  Cd Length: 77  Bit Score: 119.10  E-value: 2.17e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520009  25 SFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYM 101
Cdd:cd07978   1 LFTKEIRQMMYGFGDVRNPLPETVDLLEEIVIEYITDLLHKAMEVAKLRGSKKISVEDILFLLRKDPKKLARVKELL 77
HFD_SPT3 cd22926
histone-fold domain found in protein SPT3 and similar proteins; SPT3, also called suppressor ...
25-105 1.31e-26

histone-fold domain found in protein SPT3 and similar proteins; SPT3, also called suppressor of Ty 3 homolog, or positive regulator of Ty transcription, is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TATA binding protein (TBP) interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA (SAGA altered, SPT8 absent), an altered form of SAGA, may be involved in positive transcriptional regulation. Besides lacking SPT8, SALSA contains an SPT7 subunit that is truncated. SPT3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK (SAGA-like) is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. SPT3 regulates Ty1 as well as mating factor genes.


Pssm-ID: 467051  Cd Length: 81  Bit Score: 101.12  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520009  25 SFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYMFIR 104
Cdd:cd22926   1 SYRTEIQQMMFVLGDVRDPLPETVDLVEDIVRQQMILLLYQASELASSRGSRQITPEDVLFLLRHDKVKLNRLLTYLKWK 80

                .
gi 30520009 105 D 105
Cdd:cd22926  81 D 81
TAF19 COG5248
Transcription initiation factor TFIID, subunit TAF13 [Transcription];
18-96 1.39e-08

Transcription initiation factor TFIID, subunit TAF13 [Transcription];


Pssm-ID: 227573  Cd Length: 126  Bit Score: 52.66  E-value: 1.39e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520009  18 RNAGKTISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGArvISAEDLLFLMRKDKKKLRR 96
Cdd:COG5248   3 REARRVNLFMKDIKSLMYAYGDVVAPRYDTAEALHEYVLDYMSILCTNAHNMAQVRNK--TKTEDFKFALRRDPKKLGR 79
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH