Dcp1 (mRNA-decapping enzyme subunit 1) family protein similar to Mus musculus mRNA-decapping enzyme 1A/1B that may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
6-126
3.39e-65
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.
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Pssm-ID: 197362 Cd Length: 121 Bit Score: 204.68 E-value: 3.39e-65
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
6-126
3.39e-65
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.
Pssm-ID: 197362 Cd Length: 121 Bit Score: 204.68 E-value: 3.39e-65
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
9-124
1.48e-60
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two proteins have been identified that are essential for decapping, Dcp1 (this family) and Dcp2 (pfam05026). The precise role of these proteins in the decapping reaction have not been established. Evidence suggests that the Dcp1 may enhance the function of Dcp2.
Pssm-ID: 461816 Cd Length: 117 Bit Score: 192.77 E-value: 1.48e-60
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of ...
6-126
3.39e-65
mRNA decapping enzyme 1 (Dcp1); mRNA decapping enzyme 1 (Dcp1), together with Dcp2, is part of the decapping complex which catalyzes the removal of the 5' cap structure of mRNA. This decapping reaction is an essential step in mRNA degradation, by exposing the 5' end for exonucleolytic digestion. Dcp1 binds to the N-terminal helical domain of catalytic subunit Dcp2 and enhances its function by promoting Dsp2's closed conformation which is catalytically more active.
Pssm-ID: 197362 Cd Length: 121 Bit Score: 204.68 E-value: 3.39e-65
Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The ...
11-126
2.44e-62
Decapping enzyme EVH1-like domain; Dcp1 is a small protein containing an EVH1 domain. The Dcp1-Dcp2 complex plays a critical step in mRNA degradation with the removal of the 50 cap structure. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. The interface of Dcp1 and Dcp2 is not fully conserved and in higher eukaryotes it requires an additional factor. The proline-rich sequence (PRS)-binding sites in Dcp1p indicates that it belongs to a novel class of EVH1 domains. Dcp1 has 2 prominent sites,one required for the function of the Dcp1p-Dcp2p complex, and the other, the PRS-binding site of EVH1 domains, a binding site for decapping regulatory proteins. It also has a conserved hydrophobic patch is shown to be critical for decapping. The EVH1 domains are part of the PH domain superamily.
Pssm-ID: 270003 Cd Length: 116 Bit Score: 197.36 E-value: 2.44e-62
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two ...
9-124
1.48e-60
Dcp1-like decapping family; An essential step in mRNA turnover is decapping. In yeast, two proteins have been identified that are essential for decapping, Dcp1 (this family) and Dcp2 (pfam05026). The precise role of these proteins in the decapping reaction have not been established. Evidence suggests that the Dcp1 may enhance the function of Dcp2.
Pssm-ID: 461816 Cd Length: 117 Bit Score: 192.77 E-value: 1.48e-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.
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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.
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
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
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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
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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
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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