C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
758-905
5.75e-59
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.
:
Pssm-ID: 211397 Cd Length: 134 Bit Score: 197.89 E-value: 5.75e-59
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
110-332
5.45e-48
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.
:
Pssm-ID: 397130 Cd Length: 203 Bit Score: 169.85 E-value: 5.45e-48
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
758-905
5.75e-59
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.
Pssm-ID: 211397 Cd Length: 134 Bit Score: 197.89 E-value: 5.75e-59
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
110-332
5.45e-48
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.
Pssm-ID: 397130 Cd Length: 203 Bit Score: 169.85 E-value: 5.45e-48
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
111-332
6.43e-42
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA. Ponting (TiBS) "Novel eIF4G domain homologues (in press)
Pssm-ID: 214713 Cd Length: 200 Bit Score: 152.13 E-value: 6.43e-42
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
576-684
8.39e-12
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and/or regions similar to MIF4G domains Ponting (TIBS) "Novel eIF4G domain homologues" in press
Pssm-ID: 214714 Cd Length: 113 Bit Score: 63.03 E-value: 8.39e-12
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
758-905
5.75e-59
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.
Pssm-ID: 211397 Cd Length: 134 Bit Score: 197.89 E-value: 5.75e-59
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
110-332
5.45e-48
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.
Pssm-ID: 397130 Cd Length: 203 Bit Score: 169.85 E-value: 5.45e-48
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
111-332
6.43e-42
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA. Ponting (TiBS) "Novel eIF4G domain homologues (in press)
Pssm-ID: 214713 Cd Length: 200 Bit Score: 152.13 E-value: 6.43e-42
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
576-684
8.39e-12
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and/or regions similar to MIF4G domains Ponting (TIBS) "Novel eIF4G domain homologues" in press
Pssm-ID: 214714 Cd Length: 113 Bit Score: 63.03 E-value: 8.39e-12
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
763-898
2.85e-07
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of several translation initiation factors, including the epsilon chain of eIF2b, where it has been found to catalyze the conversion of eIF2.GDP to its active eIF2.GTP form. The structure of the domain resembles that of a set of concatenated HEAT repeats.
Pssm-ID: 211395 Cd Length: 135 Bit Score: 50.55 E-value: 2.85e-07
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
801-911
6.43e-07
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats.
Pssm-ID: 211396 Cd Length: 169 Bit Score: 50.34 E-value: 6.43e-07
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
778-912
1.38e-04
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase acceleration protein (GAP), as well as a GDP dissociation inhibitor (GDI) during translational initiation in eukaryotes. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.
Pssm-ID: 211399 Cd Length: 157 Bit Score: 43.37 E-value: 1.38e-04
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
825-914
5.29e-03
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; eIF5C appears to be essential for the initiation of protein translation; its actual function, and specifically that of the C-terminal W2 domain, are not well understood. The Drosophila ortholog, kra (krasavietz) or exba (extra bases), may be involved in translational inhibition in neural development. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.
Pssm-ID: 211398 [Multi-domain] Cd Length: 194 Bit Score: 39.12 E-value: 5.29e-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,
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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,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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the domain superfamily to which the specific and non-specific hits belong
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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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