Species | SFDP01 sp004558185 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; SFDP01; SFDP01 sp004558185 | |||||||||||
CAZyme ID | MGYG000003613_00496 | |||||||||||
CAZy Family | GT11 | |||||||||||
CAZyme Description | O-antigen biosynthesis glycosyltransferase WbnK | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16424; End: 17284 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT11 | 4 | 279 | 1.7e-62 | 0.9855072463768116 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11301 | Fut1_Fut2_like | 1.45e-45 | 1 | 274 | 1 | 264 | Alpha-1,2-fucosyltransferase. Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. 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. |
pfam01531 | Glyco_transf_11 | 6.92e-24 | 5 | 280 | 4 | 297 | Glycosyl transferase family 11. This family contains several fucosyl transferase enzymes. |
cd11548 | NodZ_like | 1.65e-07 | 8 | 254 | 7 | 282 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUF69008.1 | 5.11e-41 | 4 | 263 | 3 | 265 |
AKF24141.1 | 3.36e-39 | 4 | 263 | 3 | 269 |
QXD33210.1 | 5.09e-38 | 4 | 280 | 3 | 291 |
AMV31835.1 | 1.11e-36 | 7 | 280 | 25 | 301 |
QTL97698.1 | 2.08e-36 | 4 | 263 | 3 | 252 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q58YV9 | 5.40e-20 | 7 | 263 | 5 | 282 | O-antigen biosynthesis glycosyltransferase WbnK OS=Escherichia coli OX=562 GN=wbnK PE=1 SV=1 |
Q866C9 | 5.11e-06 | 117 | 272 | 167 | 336 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Lagothrix lagotricha OX=9519 GN=FUT1 PE=3 SV=1 |
Q866C7 | 6.83e-06 | 117 | 272 | 167 | 336 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Ateles belzebuth OX=9507 GN=FUT1 PE=3 SV=1 |
Q866D2 | 9.11e-06 | 117 | 272 | 166 | 335 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Leontocebus fuscicollis OX=9487 GN=FUT1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000049 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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