Species | Parabacteroides faecis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides faecis | |||||||||||
CAZyme ID | MGYG000000174_03576 | |||||||||||
CAZy Family | GT11 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 110476; End: 112113 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT11 | 12 | 289 | 8.2e-65 | 0.9927536231884058 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11301 | Fut1_Fut2_like | 9.91e-53 | 12 | 271 | 3 | 253 | 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 | 1.42e-21 | 2 | 289 | 23 | 297 | Glycosyl transferase family 11. This family contains several fucosyl transferase enzymes. |
cd04434 | LanC_like | 0.001 | 316 | 430 | 1 | 123 | Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions. |
cd04791 | LanC_SerThrkinase | 0.002 | 314 | 369 | 44 | 92 | Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown. |
cd11548 | NodZ_like | 0.004 | 98 | 262 | 119 | 284 | 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 |
---|---|---|---|---|---|
BCI63862.1 | 2.01e-63 | 13 | 289 | 4 | 284 |
QXP69641.1 | 3.61e-58 | 13 | 289 | 3 | 296 |
QXP67481.1 | 3.61e-58 | 13 | 289 | 3 | 296 |
AII69332.1 | 6.38e-58 | 13 | 289 | 3 | 278 |
ALA75149.1 | 6.38e-58 | 13 | 289 | 3 | 278 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q58YV9 | 4.55e-32 | 16 | 289 | 5 | 302 | O-antigen biosynthesis glycosyltransferase WbnK OS=Escherichia coli OX=562 GN=wbnK PE=1 SV=1 |
Q866E7 | 7.79e-15 | 2 | 289 | 72 | 353 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Aotus nancymaae OX=37293 GN=FUT1 PE=3 SV=1 |
Q866E6 | 7.79e-15 | 2 | 289 | 72 | 353 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Aotus azarae OX=30591 GN=FUT1 PE=3 SV=1 |
Q866E1 | 1.40e-14 | 2 | 289 | 72 | 353 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Alouatta belzebul OX=30590 GN=FUT1 PE=3 SV=1 |
Q866C9 | 1.87e-14 | 2 | 289 | 72 | 353 | Galactoside alpha-(1,2)-fucosyltransferase 1 OS=Lagothrix lagotricha OX=9519 GN=FUT1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000050 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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