Species | Uncinocarpus reesii | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii | |||||||||||
CAZyme ID | EEP82810.1 | |||||||||||
CAZy Family | GT66 | |||||||||||
CAZyme Description | conserved hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
310354 | Glyco_transf_90 | 9.58e-23 | 144 | 334 | 122 | 312 | Glycosyl transferase family 90. This family of glycosyl transferases are specifically (mannosyl) glucuronoxylomannan/galactoxylomannan -beta 1,2-xylosyltransferases, EC:2.4.2.-. |
214773 | CAP10 | 6.32e-19 | 108 | 342 | 3 | 250 | Putative lipopolysaccharide-modifying enzyme. |
340831 | GT4_PimA-like | 0.005 | 285 | 330 | 313 | 359 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.61e-158 | 1 | 369 | 31 | 447 | |
4.95e-151 | 1 | 368 | 38 | 450 | |
4.95e-151 | 1 | 368 | 38 | 450 | |
5.66e-150 | 1 | 368 | 38 | 450 | |
5.66e-150 | 1 | 368 | 38 | 450 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.37e-07 | 79 | 337 | 110 | 371 | Crystal structure of Drosophila Poglut1 (Rumi) complexed with its glycoprotein product (glucosylated EGF repeat) and UDP [Drosophila melanogaster],5F85_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat) and UDP [Drosophila melanogaster],5F86_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat) [Drosophila melanogaster],5F87_A Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_B Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_C Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_D Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_E Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster],5F87_F Crystal structure of Drosophila Poglut1 (Rumi) complexed with UDP [Drosophila melanogaster] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.97e-07 | 144 | 346 | 177 | 387 | O-glucosyltransferase rumi homolog OS=Anopheles gambiae OX=7165 GN=AGAP004267 PE=3 SV=1 |
|
7.16e-07 | 79 | 344 | 120 | 388 | O-glucosyltransferase rumi OS=Drosophila pseudoobscura pseudoobscura OX=46245 GN=rumi PE=3 SV=1 |
|
7.19e-07 | 79 | 337 | 122 | 383 | O-glucosyltransferase rumi OS=Drosophila melanogaster OX=7227 GN=rumi PE=1 SV=1 |
|
1.96e-06 | 94 | 344 | 216 | 466 | Protein O-glucosyltransferase 2 OS=Mus musculus OX=10090 GN=Poglut2 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000040 | 0.000001 |
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