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Conserved domains on  [gi|85726390|ref|NP_573248|]
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Spt7 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_SUPT7L cd06847
histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, ...
 140-227 7.78e-21

histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, also called STAGA complex 65 subunit gamma, adenocarcinoma antigen ART1, SPTF-associated factor 65 gamma, or STAF65gamma, is the ortholog of yeast SPT7 in mammalian cells. It is highly similar to yeast SPT7 but lacks the N-terminal SPT7 bromodomain. SUPT7L is a protein component specific to STAGA (SPT3-TAF9-GCN5 Acetyltransferase)-type complexes. It plays an essential role for the integrity of the STAGA complex.


:

Pssm-ID: 467022  Cd Length: 86  Bit Score: 85.70  E-value: 7.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726390 140 PSSACRQAMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSFIGEYRGYYDSQPRlqNSTVLQLVPLERAHFAQTGTS 219
Cdd:cd06847   1 DEESVRQLLRKSVAAILAHAGFDSASESALEVLTDVLDEFLRKFTRLLRSAVDREAL--SGETGFPDILERVLHEMGIGG 78


                ....*...
gi 85726390 220 LTQVHNYY 227
Cdd:cd06847  79 ISSLHEYY 86
 
Name Accession Description Interval E-value
HFD_SUPT7L cd06847
histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, ...
 140-227 7.78e-21

histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, also called STAGA complex 65 subunit gamma, adenocarcinoma antigen ART1, SPTF-associated factor 65 gamma, or STAF65gamma, is the ortholog of yeast SPT7 in mammalian cells. It is highly similar to yeast SPT7 but lacks the N-terminal SPT7 bromodomain. SUPT7L is a protein component specific to STAGA (SPT3-TAF9-GCN5 Acetyltransferase)-type complexes. It plays an essential role for the integrity of the STAGA complex.


Pssm-ID: 467022  Cd Length: 86  Bit Score: 85.70  E-value: 7.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726390 140 PSSACRQAMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSFIGEYRGYYDSQPRlqNSTVLQLVPLERAHFAQTGTS 219
Cdd:cd06847   1 DEESVRQLLRKSVAAILAHAGFDSASESALEVLTDVLDEFLRKFTRLLRSAVDREAL--SGETGFPDILERVLHEMGIGG 78


                ....*...
gi 85726390 220 LTQVHNYY 227
Cdd:cd06847  79 ISSLHEYY 86
 
Name Accession Description Interval E-value
HFD_SUPT7L cd06847
histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, ...
 140-227 7.78e-21

histone-fold domain found in Suppressor of Ty 7-like (SUPT7L) and similar proteins; SUPT7L, also called STAGA complex 65 subunit gamma, adenocarcinoma antigen ART1, SPTF-associated factor 65 gamma, or STAF65gamma, is the ortholog of yeast SPT7 in mammalian cells. It is highly similar to yeast SPT7 but lacks the N-terminal SPT7 bromodomain. SUPT7L is a protein component specific to STAGA (SPT3-TAF9-GCN5 Acetyltransferase)-type complexes. It plays an essential role for the integrity of the STAGA complex.


Pssm-ID: 467022  Cd Length: 86  Bit Score: 85.70  E-value: 7.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726390 140 PSSACRQAMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSFIGEYRGYYDSQPRlqNSTVLQLVPLERAHFAQTGTS 219
Cdd:cd06847   1 DEESVRQLLRKSVAAILAHAGFDSASESALEVLTDVLDEFLRKFTRLLRSAVDREAL--SGETGFPDILERVLHEMGIGG 78


                ....*...
gi 85726390 220 LTQVHNYY 227
Cdd:cd06847  79 ISSLHEYY 86
HFD_SPT7 cd22927
histone-fold domain found in protein SPT7 and similar proteins; SPT7, also called suppressor ...
 136-194 2.25e-05

histone-fold domain found in protein SPT7 and similar proteins; SPT7, also called suppressor of Ty 7 homolog, 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. 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. SPT7 is transcriptional activator of TY elements and other genes.


Pssm-ID: 467052  Cd Length: 117  Bit Score: 43.30  E-value: 2.25e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 85726390 136 YPEIPSSACRQAMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSFIGEYRGYYDSQ 194
Cdd:cd22927   4 GPVLSEEAARAALRRSVAKLLAHAGFEGAQPSALDVLTDIAADYLSNLGRTLRLYLDRY 62
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 147-183 8.64e-05

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: 39.89  E-value: 8.64e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 85726390 147 AMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSF 183
Cdd:cd00076   1 LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEEL 37
HFD_TAF8 cd22918
histone-fold domain found in transcription initiation factor TFIID subunit 8 (TAF8) and ...
 143-230 4.20e-03

histone-fold domain found in transcription initiation factor TFIID subunit 8 (TAF8) and similar proteins; TAF8, also called TATA Binding Protein (TBP) associated factor 8, protein taube nuss, TBP-associated factor 43 kDa, TBP-associated factor 8, or transcription initiation factor TFIID 43 kDa subunit (TAFII-43, TAFII43), 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. TAF8 mediates both basal and activator-dependent transcription. It is involved in the differentiation of preadipocyte fibroblasts to adipocytes, however, it does not seem to play a role in differentiation of myoblasts. TAF8 is required for the integration of TAF10 in the TAF complex. It may be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo.


Pssm-ID: 467043  Cd Length: 84  Bit Score: 35.99  E-value: 4.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85726390 143 ACRQAMRKVMCGMLRLAGFTDCSESAVQLLTDATEEFLRSFIGEYRGYYDSQPRLQ---NSTVLQLVplerahfaQTGTS 219
Cdd:cd22918   1 ARRRVLQVAVAALCLEAGFESAEKSALETLTEMLQSYLTEIGRSSKAYCELAGRTEptlSDVVLALI--------DMGIN 72

                        90
                ....*....|.
gi 85726390 220 LTQVHNYYKHK 230
Cdd:cd22918  73 VDSLPEYAKRP 83
 
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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