Species | Saprolegnia diclina | |||||||||||
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Lineage | Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina | |||||||||||
CAZyme ID | SDRG_07118-t26_1-p1 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.50:13 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 72 | 744 | 1.9e-219 | 0.995475113122172 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
398659 | NAGLU | 8.65e-173 | 131 | 464 | 2 | 331 | Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold. |
404009 | NAGLU_C | 1.41e-80 | 474 | 740 | 1 | 258 | Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold. |
404008 | NAGLU_N | 5.32e-17 | 33 | 106 | 1 | 72 | Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 13 | 762 | 9 | 754 | |
0.0 | 22 | 761 | 15 | 744 | |
1.75e-285 | 12 | 746 | 13 | 747 | |
2.31e-282 | 14 | 751 | 16 | 753 | |
1.09e-271 | 19 | 751 | 18 | 753 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.03e-166 | 28 | 746 | 2 | 711 | Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
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4.51e-97 | 23 | 746 | 162 | 877 | Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with 2-acetamido-1,2-dideoxynojirmycin [Clostridium perfringens],2VCA_A Family 89 glycoside hydrolase from Clostridium perfringens in complex with beta-N-acetyl-D-glucosamine [Clostridium perfringens],2VCB_A Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with PUGNAc [Clostridium perfringens],2VCC_A Family 89 Glycoside Hydrolase from Clostridium perfringens [Clostridium perfringens] |
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5.25e-97 | 23 | 746 | 170 | 885 | Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124] |
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5.03e-96 | 23 | 746 | 185 | 900 | CpGH89 (E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.10e-165 | 28 | 746 | 25 | 734 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
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6.37e-159 | 74 | 746 | 94 | 804 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000204 | 0.999756 | CS pos: 20-21. Pr: 0.9788 |
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