Species | Blastomyces dermatitidis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces dermatitidis | |||||||||||
CAZyme ID | EEQ92382.2 | |||||||||||
CAZy Family | GH55 | |||||||||||
CAZyme Description | alpha-N-acetylglucosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 87 | 752 | 1.1e-196 | 0.9834087481146304 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
398659 | NAGLU | 9.25e-180 | 147 | 485 | 1 | 333 | 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 | 4.38e-84 | 493 | 754 | 1 | 256 | 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 | 1.95e-19 | 44 | 132 | 1 | 81 | 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 |
---|---|---|---|---|---|
5.54e-264 | 42 | 736 | 33 | 729 | |
1.66e-253 | 28 | 771 | 9 | 751 | |
3.36e-250 | 21 | 771 | 1 | 755 | |
4.38e-243 | 29 | 771 | 10 | 751 | |
6.15e-243 | 33 | 766 | 21 | 785 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.41e-140 | 78 | 717 | 40 | 664 | Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
|
5.10e-80 | 77 | 763 | 201 | 871 | 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] |
|
5.77e-80 | 77 | 763 | 209 | 879 | Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124] |
|
4.92e-79 | 77 | 763 | 224 | 894 | 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 |
---|---|---|---|---|---|---|
2.02e-141 | 28 | 717 | 13 | 687 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
|
6.26e-114 | 31 | 713 | 37 | 753 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.589211 | 0.410778 |
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