Species | Aspergillus fumigatus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus | |||||||||||
CAZyme ID | AFUB_025270-T-p1 | |||||||||||
CAZy Family | GH106 | |||||||||||
CAZyme Description | Protein of unknown function | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 61 | 741 | 3.5e-215 | 0.9909502262443439 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
398659 | NAGLU | 0.0 | 129 | 466 | 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 | 7.58e-97 | 474 | 731 | 1 | 250 | 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 | 3.31e-22 | 22 | 114 | 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 |
---|---|---|---|---|---|
0.0 | 3 | 750 | 6 | 753 | |
0.0 | 10 | 724 | 22 | 733 | |
0.0 | 5 | 750 | 6 | 752 | |
2.54e-315 | 3 | 750 | 8 | 749 | |
6.58e-315 | 4 | 750 | 8 | 755 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.04e-142 | 86 | 746 | 66 | 715 | Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
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4.10e-107 | 19 | 742 | 169 | 872 | 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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4.85e-107 | 19 | 742 | 177 | 880 | 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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4.87e-106 | 19 | 742 | 192 | 895 | 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 |
---|---|---|---|---|---|---|
4.12e-142 | 86 | 746 | 89 | 738 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
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7.21e-136 | 27 | 741 | 52 | 803 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000237 | 0.999718 | CS pos: 18-19. Pr: 0.9815 |
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