Species | Phytophthora capsici | |||||||||||
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Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici | |||||||||||
CAZyme ID | KAG1708646.1 | |||||||||||
CAZy Family | GT41 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
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 | 80 | 759 | 2.7e-214 | 0.9924585218702866 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
398659 | NAGLU | 1.03e-178 | 138 | 476 | 2 | 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 | 3.30e-86 | 484 | 756 | 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 | 6.74e-23 | 40 | 122 | 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 |
---|---|---|---|---|---|
8.36e-310 | 24 | 772 | 13 | 746 | |
1.11e-304 | 36 | 779 | 22 | 741 | |
1.45e-246 | 36 | 759 | 31 | 745 | |
6.43e-228 | 36 | 762 | 28 | 748 | |
1.67e-222 | 36 | 762 | 30 | 747 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.61e-153 | 40 | 762 | 7 | 711 | Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
|
2.91e-84 | 43 | 707 | 175 | 821 | 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] |
|
3.32e-84 | 43 | 707 | 183 | 829 | 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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2.94e-83 | 43 | 707 | 198 | 844 | 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 |
---|---|---|---|---|---|---|
1.17e-167 | 40 | 762 | 47 | 804 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
|
3.32e-152 | 1 | 762 | 1 | 734 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
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0.000196 | 0.999767 | CS pos: 24-25. Pr: 0.9635 |
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