GDP-fucose protein O-fucosyltransferase 2 (POFUT2) catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
45-424
0e+00
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
:
Pssm-ID: 211384 Cd Length: 374 Bit Score: 594.25 E-value: 0e+00
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
45-424
0e+00
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
Pssm-ID: 211384 Cd Length: 374 Bit Score: 594.25 E-value: 0e+00
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
45-410
1.36e-43
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing the enzyme responsible for adding O-fucose to EGF (epidermal growth factor-like) repeats. Six highly conserved cysteines are present in O-FucT-1 as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteriztic of several glycosyltransferase families. The enzyme is a membrane-bound protein released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese.
Pssm-ID: 463023 [Multi-domain] Cd Length: 247 Bit Score: 153.22 E-value: 1.36e-43
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
45-424
0e+00
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
Pssm-ID: 211384 Cd Length: 374 Bit Score: 594.25 E-value: 0e+00
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
45-410
1.36e-43
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing the enzyme responsible for adding O-fucose to EGF (epidermal growth factor-like) repeats. Six highly conserved cysteines are present in O-FucT-1 as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteriztic of several glycosyltransferase families. The enzyme is a membrane-bound protein released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese.
Pssm-ID: 463023 [Multi-domain] Cd Length: 247 Bit Score: 153.22 E-value: 1.36e-43
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
243-412
2.92e-27
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
Pssm-ID: 211383 Cd Length: 206 Bit Score: 107.89 E-value: 2.92e-27
GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or ...
80-412
1.44e-08
GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or O-FucT-1) adds O-fucose to EGF (epidermal growth factor-like) repeats. The O-fucsosylation of the Notch receptor signaling protein is dependent on this enzyme, which requires GDP-fucose as a substrate. O-fucose residues added to the target of O-FucT-1 may be further elongated by other glycosyltransferases. On top of O-fucosylation, O-FucT-1 may have other functions such as the regulation of the Notch receptor exit from the ER. Six highly conserved cysteines are present in O-FucT-1, which is a soluble ER protein, as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteristic of several glycosyltransferase families. The membrane-bound pre-protein is released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese. O-FucT-1 is similar to family 1 glycosyltransferases (GT1).
Pssm-ID: 211388 Cd Length: 347 Bit Score: 56.09 E-value: 1.44e-08
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
295-400
1.98e-05
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
Pssm-ID: 211389 [Multi-domain] Cd Length: 287 Bit Score: 46.21 E-value: 1.98e-05
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
