Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.006G090800.1 |
Family | GT68 |
Protein Properties | Length: 522 Molecular Weight: 59149.2 Isoelectric Point: 7.9666 |
Chromosome | Chromosome/Scaffold: 06 Start: 32715908 End: 32719985 |
Description | O-fucosyltransferase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT68 | 201 | 496 | 0 |
LNRVLVIPGSKFDYQYNLVLDIEHINECIGRKTVISFKNFMELKKNHARIDKFICYFSIPLPCYTDEDHLKQLKSLGISMGKVETAWKSEDIENPSPKTV KDVEEKFGTKEDVIAIGDVFFANVEKDWVLQPRGPIAHKCKILIEPSKLILLTAQRFIQTFLGSGFVALHFRRHGFLKFCNAKKPSCFYPIPQAADCIRQ MVEKANTSVIYLSTDAAESETSLLQSMLVMNGKTIPLVKRPPRDSAEKWDSLLYRHGLDGDDQVEAMLDKTICAMASVFIGAPGSTFTEDILRLRK |
Full Sequence |
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Protein Sequence Length: 522 Download |
MARDSPNEDD DHENLIHQNK DKSASFRIEE LQSPIRRRFS KGHYLFAAIV TVISLVATIY 60 LFFSSKICGT TSDRIKESQL RALYLLNKQR SSLFDLWNHT FGTSNNITAV RFDQIKASLL 120 DQITLNRHIK DTLLSTENGT VSVPIVNGSE ICLKIDPKSS KRRTIEWKPD PNKFLFAICL 180 SGQMSNHLIC LEKHMFFAAV LNRVLVIPGS KFDYQYNLVL DIEHINECIG RKTVISFKNF 240 MELKKNHARI DKFICYFSIP LPCYTDEDHL KQLKSLGISM GKVETAWKSE DIENPSPKTV 300 KDVEEKFGTK EDVIAIGDVF FANVEKDWVL QPRGPIAHKC KILIEPSKLI LLTAQRFIQT 360 FLGSGFVALH FRRHGFLKFC NAKKPSCFYP IPQAADCIRQ MVEKANTSVI YLSTDAAESE 420 TSLLQSMLVM NGKTIPLVKR PPRDSAEKWD SLLYRHGLDG DDQVEAMLDK TICAMASVFI 480 GAPGSTFTED ILRLRKGWET ASSCDEYLCH GEEPNFIASD K* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11548 | NodZ_like | 0.005 | 343 | 497 | 159 | + 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. | ||
cd11296 | O-FucT_like | 0.0003 | 174 | 208 | 35 | + 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 | 2.0e-7 | 197 | 488 | 326 | + 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. | ||
cd11298 | O-FucT-2 | 7.0e-9 | 362 | 488 | 129 | + 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. | ||
cd11296 | O-FucT_like | 1.0e-18 | 333 | 495 | 181 | + 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. |
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 | AAD50008.1 | 0 | 1 | 521 | 1 | 594 | AC007651_3 Hypothetical Protein [Arabidopsis thaliana] |
RefSeq | NP_173170.2 | 0 | 1 | 521 | 1 | 564 | unknown protein [Arabidopsis thaliana] |
RefSeq | NP_199853.1 | 0 | 1 | 521 | 1 | 566 | unknown protein [Arabidopsis thaliana] |
RefSeq | XP_002264087.1 | 0 | 1 | 521 | 1 | 559 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002303337.1 | 0 | 1 | 521 | 1 | 527 | predicted protein [Populus trichocarpa] |
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 | 4ap6_D | 0.0007 | 362 | 488 | 277 | 383 | A Chain A, Crystal Structure Of Human Pofut2 E54a Mutant In Complex With Gdp- Fucose |
PDB | 4ap6_C | 0.0007 | 362 | 488 | 277 | 383 | A Chain A, Crystal Structure Of Human Pofut2 E54a Mutant In Complex With Gdp- Fucose |
PDB | 4ap6_B | 0.0007 | 362 | 488 | 277 | 383 | A Chain A, Crystal Structure Of Human Pofut2 E54a Mutant In Complex With Gdp- Fucose |
PDB | 4ap6_A | 0.0007 | 362 | 488 | 277 | 383 | A Chain A, Crystal Structure Of Human Pofut2 E54a Mutant In Complex With Gdp- Fucose |
PDB | 4ap5_B | 0.0008 | 362 | 488 | 263 | 369 | A Chain A, Crystal Structure Of Human Pofut2 |