MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
791-1019
3.50e-62
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: 211.07 E-value: 3.50e-62
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
1464-1592
7.03e-48
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: 167.46 E-value: 7.03e-48
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
1571-1617
8.89e-05
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.
The actual alignment was detected with superfamily member cd11560:
Pssm-ID: 473053 [Multi-domain] Cd Length: 194 Bit Score: 45.28 E-value: 8.89e-05
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
791-1019
3.50e-62
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: 211.07 E-value: 3.50e-62
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
792-1016
1.34e-49
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: 174.86 E-value: 1.34e-49
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
1464-1592
7.03e-48
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: 167.46 E-value: 7.03e-48
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
1258-1370
1.30e-34
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: 128.52 E-value: 1.30e-34
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
1571-1617
8.89e-05
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: 45.28 E-value: 8.89e-05
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
155-370
6.18e-04
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: 44.52 E-value: 6.18e-04
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
791-1019
3.50e-62
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: 211.07 E-value: 3.50e-62
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
792-1016
1.34e-49
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: 174.86 E-value: 1.34e-49
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
1464-1592
7.03e-48
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: 167.46 E-value: 7.03e-48
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
1258-1370
1.30e-34
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: 128.52 E-value: 1.30e-34
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
1460-1586
3.22e-19
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: 85.61 E-value: 3.22e-19
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
1500-1619
1.61e-15
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: 75.76 E-value: 1.61e-15
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
1478-1619
2.23e-08
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: 54.93 E-value: 2.23e-08
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
1571-1617
8.89e-05
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: 45.28 E-value: 8.89e-05
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
155-370
6.18e-04
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: 44.52 E-value: 6.18e-04
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
5-343
6.06e-03
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.29 E-value: 6.06e-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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
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
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
