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CAZyme Information: OJD11313.1

You are here: Home > Sequence: OJD11313.1

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 Blastomyces percursus
Lineage Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces percursus
CAZyme ID OJD11313.1
CAZy Family AA3
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
563 63298.03 4.6895
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_BpercursusEI222 10384 N/A 99 10285
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in OJD11313.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH89 30 334 6.6e-90 0.45098039215686275

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
398659 NAGLU 5.11e-139 1 323 7 333
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 4.78e-44 335 539 32 250
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.50e-151 1 527 142 729
2.97e-145 1 562 133 751
8.56e-144 1 532 133 719
5.18e-142 9 562 152 747
8.19e-142 1 535 134 723

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.42e-85 2 500 114 641
Crystal structure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
1.11e-37 2 505 277 811
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]
1.12e-37 2 505 285 819
Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
6.69e-37 2 505 300 834
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
2.61e-85 2 500 137 664
Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2
8.13e-66 1 543 163 788
Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.994804 0.005227

TMHMM  Annotations      help

There is no transmembrane helices in OJD11313.1.