Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
616-857
3.11e-111
Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.
:
Pssm-ID: 461598 [Multi-domain] Cd Length: 264 Bit Score: 341.17 E-value: 3.11e-111
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
258-349
6.34e-42
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.
:
Pssm-ID: 462195 Cd Length: 90 Bit Score: 147.80 E-value: 6.34e-42
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
616-857
3.11e-111
Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.
Pssm-ID: 461598 [Multi-domain] Cd Length: 264 Bit Score: 341.17 E-value: 3.11e-111
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
258-349
6.34e-42
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.
Pssm-ID: 462195 Cd Length: 90 Bit Score: 147.80 E-value: 6.34e-42
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
651-750
8.83e-38
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), 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. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.
Pssm-ID: 467027 [Multi-domain] Cd Length: 100 Bit Score: 136.20 E-value: 8.83e-38
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
40-244
4.13e-03
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.06 E-value: 4.13e-03
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
616-857
3.11e-111
Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.
Pssm-ID: 461598 [Multi-domain] Cd Length: 264 Bit Score: 341.17 E-value: 3.11e-111
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
258-349
6.34e-42
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.
Pssm-ID: 462195 Cd Length: 90 Bit Score: 147.80 E-value: 6.34e-42
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
651-750
8.83e-38
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), 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. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.
Pssm-ID: 467027 [Multi-domain] Cd Length: 100 Bit Score: 136.20 E-value: 8.83e-38
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
40-244
4.13e-03
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.06 E-value: 4.13e-03
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
657-793
4.71e-03
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 4.71e-03
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
659-787
6.89e-03
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 6.89e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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