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CAZyme Information: H257_10995-t26_3-p1

You are here: Home > Sequence: H257_10995-t26_3-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aphanomyces astaci
Lineage Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
CAZyme ID H257_10995-t26_3-p1
CAZy Family GT105
CAZyme Description hypothetical protein, variant 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
742 KI913144|CGC1 84804.49 6.2818
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AastaciAPO3 19584 N/A 465 19119
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.50:13

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH89 54 715 1.1e-202 0.9728506787330317

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
398659 NAGLU 1.24e-168 97 428 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-67 438 710 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.40e-263 58 742 95 775
5.23e-253 58 716 88 738
4.12e-244 58 717 85 730
6.15e-201 58 726 93 757
2.37e-192 58 716 91 748

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.00e-139 57 716 68 711
Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
6.70e-77 49 690 222 844
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]
7.52e-77 49 690 230 852
Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
6.34e-76 49 690 245 867
CpGH89 (E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.12e-152 87 716 148 804
Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
1.82e-139 57 716 91 734
Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000058 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in H257_10995-t26_3-p1.