y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 477820 |
Family | GT65 |
Protein Properties | Length: 446 Molecular Weight: 50731.8 Isoelectric Point: 9.5135 |
Chromosome | Chromosome/Scaffold: 3 Start: 1960289 End: 1961719 |
Description | O-fucosyltransferase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT65 | 78 | 389 | 0 |
GLNNQKIAFARACLTARMMNRTLLMPSLSASLFYKEVDKLRPIPFDKVFQLERFNSLCSGFVRLARFSDVRNRAQVFDLEKGSGRRWTVERDLEHLKQSA RNESIDEFEVIRVIGKNPFLWHDHWPVEDYAKVFECMVVVDEISREADKVVMKIREAGEAERAKLKSKTEIPGPIPFVAVHMRIEIDWMIHCKKLEQRKK VSEICSCKREIMERVGNISGLKTPTVLYLAVADTLLEEKEEDSSVLTGWRDGLIPFEKKKLGVKEEIYGKYSYLLQSAIDYEVCLRADVFVGNSFSTFSS LIVLERTQKARK |
Full Sequence |
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Protein Sequence Length: 446 Download |
MNSPLSCKNL RVFSKSVACK CLVLVGIALF YRALLLSYSP RNALSNSLLF RARHMSDSSS 60 TGGIRTDKFL EVPQIVWGLN NQKIAFARAC LTARMMNRTL LMPSLSASLF YKEVDKLRPI 120 PFDKVFQLER FNSLCSGFVR LARFSDVRNR AQVFDLEKGS GRRWTVERDL EHLKQSARNE 180 SIDEFEVIRV IGKNPFLWHD HWPVEDYAKV FECMVVVDEI SREADKVVMK IREAGEAERA 240 KLKSKTEIPG PIPFVAVHMR IEIDWMIHCK KLEQRKKVSE ICSCKREIME RVGNISGLKT 300 PTVLYLAVAD TLLEEKEEDS SVLTGWRDGL IPFEKKKLGV KEEIYGKYSY LLQSAIDYEV 360 CLRADVFVGN SFSTFSSLIV LERTQKARKL GFMSSCKDGE NKWRSYAYNL AGESKGVPRR 420 WMTNMTHSSL QAISYGSNSV SCSSG* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11302 | O-FucT-1 | 0.004 | 218 | 388 | 197 | + 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). | ||
cd11296 | O-FucT_like | 0.0002 | 69 | 121 | 54 | + 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. | ||
cd11299 | O-FucT_plant | 1.0e-14 | 78 | 384 | 333 | + GDP-fucose protein O-fucosyltransferase, plant specific subfamily. Some members of this plant-specific family of O-fucosyltransferases have been annotated as auxin-independent growth promotors. The function of the protein seems unclear. 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. | ||
cd11296 | O-FucT_like | 4.0e-22 | 200 | 384 | 190 | + 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. | ||
pfam10250 | O-FucT | 9.0e-49 | 78 | 388 | 342 | + 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 characteristic of several glycosyltransferase families. The enzyme is a membrane-bound protein released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAN72045.1 | 0 | 95 | 445 | 1 | 351 | unknown protein [Arabidopsis thaliana] |
RefSeq | NP_187183.3 | 0 | 1 | 445 | 1 | 445 | unknown protein [Arabidopsis thaliana] |
RefSeq | XP_002273827.1 | 0 | 17 | 442 | 1 | 427 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002332132.1 | 0 | 95 | 442 | 1 | 347 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531235.1 | 0 | 60 | 442 | 65 | 446 | conserved hypothetical protein [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3zy6_A | 0.0002 | 253 | 388 | 212 | 349 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 3zy5_A | 0.0002 | 253 | 388 | 212 | 349 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 3zy4_A | 0.0002 | 253 | 388 | 212 | 349 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 3zy3_B | 0.0002 | 253 | 388 | 212 | 349 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 3zy3_A | 0.0002 | 253 | 388 | 212 | 349 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |