Species | Bacteroides sp900761785 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785 | |||||||||||
CAZyme ID | MGYG000003252_04813 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 55434; End: 56627 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 22 | 143 | 4.1e-23 | 0.7411764705882353 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04179 | DPM_DPG-synthase_like | 3.38e-41 | 22 | 197 | 1 | 185 | DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily. |
pfam09835 | DUF2062 | 9.87e-21 | 278 | 396 | 19 | 137 | Uncharacterized protein conserved in bacteria (DUF2062). This domain, found in various prokaryotic proteins, has no known function. |
cd06442 | DPM1_like | 7.85e-20 | 22 | 209 | 1 | 197 | DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily. |
pfam00535 | Glycos_transf_2 | 2.27e-19 | 22 | 171 | 2 | 159 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
cd04187 | DPM1_like_bac | 8.49e-18 | 22 | 171 | 1 | 154 | Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QIU97459.1 | 1.30e-265 | 1 | 397 | 1 | 396 |
QNL40921.1 | 4.35e-264 | 3 | 397 | 2 | 396 |
SCV08080.1 | 2.52e-263 | 3 | 397 | 2 | 396 |
QRQ55492.1 | 2.52e-263 | 3 | 397 | 2 | 396 |
ALJ48662.1 | 2.52e-263 | 3 | 397 | 2 | 396 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B3VA58 | 2.83e-16 | 20 | 213 | 6 | 220 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 SV=1 |
A2EK20 | 3.77e-10 | 23 | 209 | 78 | 285 | Dolichyl-phosphate beta-glucosyltransferase ALG5B OS=Trichomonas vaginalis OX=5722 GN=ALG5B PE=1 SV=1 |
A2ELE6 | 7.04e-09 | 23 | 209 | 81 | 288 | Dolichyl-phosphate beta-glucosyltransferase ALG5C OS=Trichomonas vaginalis OX=5722 GN=ALG5C PE=1 SV=1 |
P75905 | 3.98e-07 | 20 | 104 | 77 | 165 | Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Escherichia coli (strain K12) OX=83333 GN=pgaC PE=1 SV=1 |
Q8XAR5 | 3.98e-07 | 20 | 104 | 77 | 165 | Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Escherichia coli O157:H7 OX=83334 GN=pgaC PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
start | end |
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232 | 249 |
279 | 301 |
314 | 336 |
367 | 389 |
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