Species | Magnaporthiopsis poae | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU87070.1 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | chitobiosyldiphosphodolichol beta-mannosyltransferase | |||||||||||
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 | 40 | 394 | 1.1e-131 | 0.8423529411764706 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
340843 | GT33_ALG1-like | 2.81e-174 | 36 | 392 | 1 | 347 | 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 | 4.19e-121 | 41 | 390 | 7 | 340 | transferase, transferring glycosyl groups |
223515 | RfaB | 1.54e-09 | 46 | 389 | 14 | 306 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
340831 | GT4_PimA-like | 1.49e-07 | 50 | 388 | 15 | 296 | 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 | 0.001 | 169 | 389 | 18 | 217 | 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 |
---|---|---|---|---|---|
9.73e-223 | 5 | 396 | 4 | 391 | |
4.17e-151 | 18 | 395 | 17 | 383 | |
1.39e-149 | 16 | 395 | 18 | 397 | |
1.39e-149 | 18 | 395 | 20 | 397 | |
3.09e-149 | 29 | 395 | 43 | 420 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.91e-100 | 13 | 395 | 15 | 382 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01551 PE=3 SV=1 |
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2.00e-79 | 43 | 388 | 44 | 372 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALG1 PE=3 SV=1 |
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8.05e-75 | 43 | 390 | 29 | 356 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg1 PE=3 SV=2 |
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3.39e-74 | 43 | 390 | 9 | 386 | UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1 |
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2.08e-73 | 35 | 388 | 48 | 382 | Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALG1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000062 | 0.000000 |
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