CCR4-NOT transcription complex subunit 1 is a scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation
CCR4-Not complex component, Not1; The Ccr4-Not complex is a global regulator of transcription ...
1993-2301
8.73e-156
CCR4-Not complex component, Not1; The Ccr4-Not complex is a global regulator of transcription that affects genes positively and negatively and is thought to regulate transcription factor TFIID.
Pssm-ID: 427680 Cd Length: 365 Bit Score: 486.25 E-value: 8.73e-156
Connector domain of NOT1; This NOT1 connector domain is one of several catalytically inactive ...
1597-1809
1.85e-60
Connector domain of NOT1; This NOT1 connector domain is one of several catalytically inactive subunits of the multisubunit CCR4-NOT complex assembly that plays a central role in post-translational gene regulation in eukaryotes. CCR4-NOT contains the catalytic center formed by two deadenylase subunits CCR4 and CAF1, and the conserved core complex which contains a minimum of four catalytically inactive subunits, NOT1, NOT2, NOT3 and CAF40/NOT9. NOT1 is the largest subunit which functions as a central scaffold for complex assembly in human orthologs. The Chaetomium thermophilum NOT1 connector domain consists of five alpha-helical hairpin repeats of the HEAT type that structurally resemble MIF4G domains, and hence is also called the MIF4G-C domain. However, NOT1 MIF4G-C does not interact with DEAD-box helicases such as DDX6 like MIF4G does. Structural conservation of this domain suggests an important role but its function is as yet unknown.
Pssm-ID: 411008 [Multi-domain] Cd Length: 202 Bit Score: 206.73 E-value: 1.85e-60
CCR4-Not complex component, Not1; The Ccr4-Not complex is a global regulator of transcription ...
1993-2301
8.73e-156
CCR4-Not complex component, Not1; The Ccr4-Not complex is a global regulator of transcription that affects genes positively and negatively and is thought to regulate transcription factor TFIID.
Pssm-ID: 427680 Cd Length: 365 Bit Score: 486.25 E-value: 8.73e-156
CCR4-NOT transcription complex subunit 1 CAF1-binding domain; This is the CAF1-binding domain ...
1083-1307
1.59e-124
CCR4-NOT transcription complex subunit 1 CAF1-binding domain; This is the CAF1-binding domain of CCR4-NOT transcription complex. It adopts a MIF4G (middle portion of eIF4G) fold.
Pssm-ID: 465111 Cd Length: 225 Bit Score: 391.10 E-value: 1.59e-124
CCR4-NOT transcription complex subunit 1 TTP binding domain; This is the TTP binding domain of ...
816-999
9.56e-97
CCR4-NOT transcription complex subunit 1 TTP binding domain; This is the TTP binding domain of CCR4-NOT transcription complex subunit 1. It adopts a MIF4G (middle portion of eIF4G) fold.
Pssm-ID: 465112 Cd Length: 183 Bit Score: 309.92 E-value: 9.56e-97
CCR4-Not complex, Not1 subunit, domain of unknown function DUF3819; This is an uncharacterized ...
1382-1528
7.37e-69
CCR4-Not complex, Not1 subunit, domain of unknown function DUF3819; This is an uncharacterized domain that is found on the CCR4-Not complex component Not1. Not1 is a global regulator of transcription that affects genes positively and negatively and is thought to regulate transcription factor TFIID.
Pssm-ID: 463726 Cd Length: 143 Bit Score: 228.17 E-value: 7.37e-69
Connector domain of NOT1; This NOT1 connector domain is one of several catalytically inactive ...
1597-1809
1.85e-60
Connector domain of NOT1; This NOT1 connector domain is one of several catalytically inactive subunits of the multisubunit CCR4-NOT complex assembly that plays a central role in post-translational gene regulation in eukaryotes. CCR4-NOT contains the catalytic center formed by two deadenylase subunits CCR4 and CAF1, and the conserved core complex which contains a minimum of four catalytically inactive subunits, NOT1, NOT2, NOT3 and CAF40/NOT9. NOT1 is the largest subunit which functions as a central scaffold for complex assembly in human orthologs. The Chaetomium thermophilum NOT1 connector domain consists of five alpha-helical hairpin repeats of the HEAT type that structurally resemble MIF4G domains, and hence is also called the MIF4G-C domain. However, NOT1 MIF4G-C does not interact with DEAD-box helicases such as DDX6 like MIF4G does. Structural conservation of this domain suggests an important role but its function is as yet unknown.
Pssm-ID: 411008 [Multi-domain] Cd Length: 202 Bit Score: 206.73 E-value: 1.85e-60
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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