Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
11-477
4.28e-118
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
:
Pssm-ID: 396873 Cd Length: 478 Bit Score: 362.86 E-value: 4.28e-118
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a ...
593-673
1.86e-21
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organizm development or host-pathogen interactions. The reaction is catalyzed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologs in bacteria and archaea. Structural analysis of a bacterial OST, undecaprenyl-diphosphooligosaccharide protein glycotransferase EC:2.4.99.19 (PglB) protein, revealed two domains: a transmembrane domain and a periplasmic domain. This entry represents the C-terminal periplasmic beta-barrel domain.
:
Pssm-ID: 465791 Cd Length: 79 Bit Score: 88.94 E-value: 1.86e-21
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
11-477
4.28e-118
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
Pssm-ID: 396873 Cd Length: 478 Bit Score: 362.86 E-value: 4.28e-118
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a ...
593-673
1.86e-21
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organizm development or host-pathogen interactions. The reaction is catalyzed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologs in bacteria and archaea. Structural analysis of a bacterial OST, undecaprenyl-diphosphooligosaccharide protein glycotransferase EC:2.4.99.19 (PglB) protein, revealed two domains: a transmembrane domain and a periplasmic domain. This entry represents the C-terminal periplasmic beta-barrel domain.
Pssm-ID: 465791 Cd Length: 79 Bit Score: 88.94 E-value: 1.86e-21
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family ...
93-461
1.72e-10
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family occur, one to three members per genome, in the same species of Euryarchaeota as contain the predicted protein-sorting enzyme archaeosortase (TIGR04125) and its cognate protein-sorting signal PGF-CTERM (TIGR04126).
Pssm-ID: 275016 [Multi-domain] Cd Length: 817 Bit Score: 64.25 E-value: 1.72e-10
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl ...
11-477
4.28e-118
Oligosaccharyl transferase STT3 subunit; This family consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines.
Pssm-ID: 396873 Cd Length: 478 Bit Score: 362.86 E-value: 4.28e-118
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a ...
593-673
1.86e-21
STT3/PglB C-terminal beta-barrel domain; Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organizm development or host-pathogen interactions. The reaction is catalyzed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologs in bacteria and archaea. Structural analysis of a bacterial OST, undecaprenyl-diphosphooligosaccharide protein glycotransferase EC:2.4.99.19 (PglB) protein, revealed two domains: a transmembrane domain and a periplasmic domain. This entry represents the C-terminal periplasmic beta-barrel domain.
Pssm-ID: 465791 Cd Length: 79 Bit Score: 88.94 E-value: 1.86e-21
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family ...
93-461
1.72e-10
oligosaccharyl transferase, archaeosortase A system-associated; Members of this protein family occur, one to three members per genome, in the same species of Euryarchaeota as contain the predicted protein-sorting enzyme archaeosortase (TIGR04125) and its cognate protein-sorting signal PGF-CTERM (TIGR04126).
Pssm-ID: 275016 [Multi-domain] Cd Length: 817 Bit Score: 64.25 E-value: 1.72e-10
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.
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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
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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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