Species | Talaromyces stipitatus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus | |||||||||||
CAZyme ID | TSTA_047750-t26_1-p1 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | alpha-N-acetylglucosaminidase, putative | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH89 | 67 | 726 | 6.7e-209 | 0.9683257918552036 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
398659 | NAGLU | 0.0 | 127 | 464 | 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 | 1.24e-88 | 472 | 724 | 1 | 242 | 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 | 2.18e-24 | 27 | 105 | 1 | 75 | 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 | 1 | 755 | 1 | 768 | |
0.0 | 11 | 754 | 8 | 754 | |
0.0 | 19 | 753 | 18 | 745 | |
0.0 | 12 | 753 | 13 | 746 | |
0.0 | 18 | 753 | 17 | 749 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.47e-148 | 26 | 699 | 6 | 662 | Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
|
2.55e-97 | 42 | 694 | 188 | 822 | 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] |
|
2.97e-97 | 42 | 694 | 196 | 830 | 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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2.85e-96 | 42 | 694 | 211 | 845 | 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 |
---|---|---|---|---|---|---|
3.50e-147 | 26 | 699 | 29 | 685 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
|
2.11e-134 | 13 | 724 | 35 | 781 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000786 | 0.999231 | CS pos: 20-21. Pr: 0.9710 |
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