translation initiation factor eIF-2B alpha/beta/delta subunit family protein similar to methylthioribose-1-phosphate isomerase that catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
S-methyl-5-thioribose-1-phosphate isomerase; The delineation of this family was based in part ...
4-187
6.26e-72
S-methyl-5-thioribose-1-phosphate isomerase; The delineation of this family was based in part on a discussion and neighbor-joining phylogenetic study, by Kyrpides and Woese, of archaeal and other proteins homologous to the alpha, beta, and delta subunits of eukaryotic initiation factor 2B (eIF-2B), a five-subunit molecule that catalyzes GTP recycling for eIF-2. This clade is now recognized to include the methionine salvage pathway enzyme MtnA. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273112 [Multi-domain] Cd Length: 335 Bit Score: 221.74 E-value: 6.26e-72
5-methylthioribose/5-deoxyribulose 1-phosphate isomerase (methionine salvage pathway), a ...
1-195
1.89e-42
5-methylthioribose/5-deoxyribulose 1-phosphate isomerase (methionine salvage pathway), a paralog of eIF-2B alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 439952 Cd Length: 343 Bit Score: 145.95 E-value: 1.89e-42
Initiation factor 2 subunit family; This family includes initiation factor 2B alpha, beta and ...
44-195
5.60e-12
Initiation factor 2 subunit family; This family includes initiation factor 2B alpha, beta and delta subunits from eukaryotes, initiation factor 2B subunits 1 and 2 from archaebacteria and some proteins of unknown function from prokaryotes. Initiation factor 2 binds to Met-tRNA, GTP and the small ribosomal subunit. Members of this family have also been characterized as 5-methylthioribose- 1-phosphate isomerases, an enzyme of the methionine salvage pathway. The crystal structure of Ypr118w, a non-essential, low-copy number gene product from Saccharomyces cerevisiae, reveals a dimeric protein with two domains and a putative active site cleft.
Pssm-ID: 395798 [Multi-domain] Cd Length: 281 Bit Score: 63.08 E-value: 5.60e-12
S-methyl-5-thioribose-1-phosphate isomerase; The delineation of this family was based in part ...
4-187
6.26e-72
S-methyl-5-thioribose-1-phosphate isomerase; The delineation of this family was based in part on a discussion and neighbor-joining phylogenetic study, by Kyrpides and Woese, of archaeal and other proteins homologous to the alpha, beta, and delta subunits of eukaryotic initiation factor 2B (eIF-2B), a five-subunit molecule that catalyzes GTP recycling for eIF-2. This clade is now recognized to include the methionine salvage pathway enzyme MtnA. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273112 [Multi-domain] Cd Length: 335 Bit Score: 221.74 E-value: 6.26e-72
5-methylthioribose/5-deoxyribulose 1-phosphate isomerase (methionine salvage pathway), a ...
1-195
1.89e-42
5-methylthioribose/5-deoxyribulose 1-phosphate isomerase (methionine salvage pathway), a paralog of eIF-2B alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 439952 Cd Length: 343 Bit Score: 145.95 E-value: 1.89e-42
eIF-2B alpha/beta/delta-related uncharacterized proteins; This model, eIF-2B_rel, describes ...
33-195
5.13e-27
eIF-2B alpha/beta/delta-related uncharacterized proteins; This model, eIF-2B_rel, describes half of a superfamily, where the other half consists of eukaryotic translation initiation factor 2B (eIF-2B) subunits alpha, beta, and delta. It is unclear whether the eIF-2B_rel set is monophyletic, or whether they are all more closely related to each other than to any eIF-2B subunit because the eIF-2B clade is highly derived. Members of this branch of the family are all uncharacterized with respect to function and are found in the Archaea, Bacteria, and Eukarya, although a number are described as putative translation intiation factor components. Proteins found by eIF-2B_rel include at least three clades, including a set of uncharacterized eukaryotic proteins, a set found in some but not all Archaea, and a set universal so far among the Archaea and closely related to several uncharacterized bacterial proteins. [Unknown function, General]
Pssm-ID: 273119 [Multi-domain] Cd Length: 303 Bit Score: 104.45 E-value: 5.13e-27
Initiation factor 2 subunit family; This family includes initiation factor 2B alpha, beta and ...
44-195
5.60e-12
Initiation factor 2 subunit family; This family includes initiation factor 2B alpha, beta and delta subunits from eukaryotes, initiation factor 2B subunits 1 and 2 from archaebacteria and some proteins of unknown function from prokaryotes. Initiation factor 2 binds to Met-tRNA, GTP and the small ribosomal subunit. Members of this family have also been characterized as 5-methylthioribose- 1-phosphate isomerases, an enzyme of the methionine salvage pathway. The crystal structure of Ypr118w, a non-essential, low-copy number gene product from Saccharomyces cerevisiae, reveals a dimeric protein with two domains and a putative active site cleft.
Pssm-ID: 395798 [Multi-domain] Cd Length: 281 Bit Score: 63.08 E-value: 5.60e-12
Translation initiation factor 2B subunit, eIF-2B alpha/beta/delta family [Translation, ...
38-172
7.78e-07
Translation initiation factor 2B subunit, eIF-2B alpha/beta/delta family [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2B subunit, eIF-2B alpha/beta/delta family is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440797 [Multi-domain] Cd Length: 304 Bit Score: 48.31 E-value: 7.78e-07
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
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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
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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