Species | Trichophyton rubrum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton rubrum | |||||||||||
CAZyme ID | KFL61272.1 | |||||||||||
CAZy Family | GT33 | |||||||||||
CAZyme Description | 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 | 5.28e-18 | 68 | 401 | 2 | 334 | Glycosyl transferase family 90. This family of glycosyl transferases are specifically (mannosyl) glucuronoxylomannan/galactoxylomannan -beta 1,2-xylosyltransferases, EC:2.4.2.-. |
214773 | CAP10 | 3.05e-15 | 157 | 384 | 3 | 245 | Putative lipopolysaccharide-modifying enzyme. |
403870 | Ank_2 | 3.51e-10 | 548 | 633 | 1 | 91 | Ankyrin repeats (3 copies). |
293786 | ANK | 1.13e-08 | 457 | 571 | 2 | 95 | ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases. |
403870 | Ank_2 | 2.45e-06 | 461 | 569 | 1 | 86 | Ankyrin repeats (3 copies). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.60e-179 | 1 | 415 | 42 | 468 | |
3.26e-176 | 1 | 415 | 38 | 452 | |
3.26e-176 | 1 | 415 | 38 | 452 | |
5.12e-176 | 1 | 413 | 31 | 446 | |
6.76e-176 | 1 | 415 | 37 | 446 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.11e-13 | 157 | 397 | 95 | 347 | human POGLUT1 in complex with Notch1 EGF12 and UDP [Homo sapiens],5L0S_A human POGLUT1 in complex with Factor VII EGF1 and UDP [Homo sapiens],5L0T_A human POGLUT1 in complex with EGF(+) and UDP [Homo sapiens],5L0U_A human POGLUT1 in complex with EGF(+) and UDP-phosphono-glucose [Homo sapiens],5L0V_A human POGLUT1 in complex with 2F-glucose modified EGF(+) and UDP [Homo sapiens],5UB5_A human POGLUT1 in complex with human Notch1 EGF12 S458T mutant and UDP [Homo sapiens] |
|
3.42e-11 | 176 | 384 | 152 | 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 |
---|---|---|---|---|---|---|
5.54e-14 | 154 | 397 | 120 | 375 | Protein O-glucosyltransferase 1 OS=Rattus norvegicus OX=10116 GN=Poglut1 PE=3 SV=1 |
|
7.37e-13 | 157 | 397 | 123 | 375 | Protein O-glucosyltransferase 1 OS=Homo sapiens OX=9606 GN=POGLUT1 PE=1 SV=1 |
|
1.74e-12 | 157 | 397 | 123 | 375 | Protein O-glucosyltransferase 1 OS=Mus musculus OX=10090 GN=Poglut1 PE=1 SV=2 |
|
3.09e-12 | 157 | 408 | 123 | 391 | Protein O-glucosyltransferase 1 OS=Bos taurus OX=9913 GN=POGLUT1 PE=2 SV=1 |
|
1.83e-10 | 176 | 384 | 164 | 383 | O-glucosyltransferase rumi OS=Drosophila melanogaster OX=7227 GN=rumi PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000071 | 0.000000 |
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