Species | Trichosporon asahii | |||||||||||
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Lineage | Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii | |||||||||||
CAZyme ID | EJT51541.1 | |||||||||||
CAZy Family | GT3 | |||||||||||
CAZyme Description | Chitobiosyldiphosphodolichol beta-mannosyltransferase [Source:UniProtKB/TrEMBL;Acc:J5TLZ8] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.142:10 | 2.4.1.-:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT33 | 48 | 462 | 3.6e-129 | 0.9905882352941177 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
340843 | GT33_ALG1-like | 2.03e-173 | 47 | 462 | 3 | 408 | chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins. This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik. |
215155 | PLN02275 | 1.74e-124 | 46 | 412 | 4 | 371 | transferase, transferring glycosyl groups |
223515 | RfaB | 2.95e-11 | 55 | 431 | 14 | 356 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
340831 | GT4_PimA-like | 8.45e-10 | 59 | 413 | 15 | 332 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. |
340816 | Glycosyltransferase_GTB-type | 4.57e-08 | 158 | 398 | 3 | 235 | glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
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5.60e-176 | 23 | 467 | 24 | 502 | |
5.60e-176 | 23 | 467 | 24 | 502 | |
7.40e-174 | 23 | 467 | 24 | 502 | |
5.99e-173 | 23 | 467 | 24 | 502 | |
1.71e-172 | 23 | 467 | 24 | 502 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.44e-80 | 45 | 461 | 30 | 457 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg1 PE=1 SV=3 |
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6.69e-77 | 29 | 467 | 16 | 463 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Pongo abelii OX=9601 GN=ALG1 PE=2 SV=1 |
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1.02e-75 | 29 | 467 | 16 | 463 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG1 PE=1 SV=2 |
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4.41e-74 | 52 | 416 | 9 | 421 | UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1 |
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1.11e-69 | 40 | 461 | 18 | 416 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000081 | 0.000003 |
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