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CAZyme Information: AO090103000218-T-p1

You are here: Home > Sequence: AO090103000218-T-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 Aspergillus oryzae
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
CAZyme ID AO090103000218-T-p1
CAZy Family GH92
CAZyme Description Has domain(s) with predicted catalytic activity, chitin binding, chitinase activity, hydrolase activity, hydrolyzing O-glycosyl compounds activity and role in carbohydrate metabolic process, chitin catabolic process
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1085 Chr8_A_oryzae_RIB40|CGC18 116735.49 4.7976
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AoryzaeRIB40 12364 510516 274 12090
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 123 461 3.2e-72 0.9256756756756757

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 1.60e-75 125 463 3 345
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753 Glyco_18 6.61e-75 125 462 3 333
Glyco_18 domain.
119351 GH18_chitolectin_chitotriosidase 8.54e-74 127 471 4 353
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
395573 Glyco_hydro_18 2.84e-69 125 461 3 305
Glycosyl hydrolases family 18.
119365 GH18_chitinase 6.72e-63 125 458 2 317
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 152 1085 24 982
9.32e-282 27 870 27 885
2.29e-218 25 656 34 672
4.77e-176 174 712 5 648
6.77e-126 27 461 87 527

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.24e-49 119 461 1 348
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5.73e-49 127 462 7 341
Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
1.43e-48 119 461 1 348
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
6.47e-48 127 462 7 341
Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
1.10e-47 122 462 1 341
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.13e-46 120 462 20 362
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
2.93e-45 118 462 19 374
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
2.98e-45 127 462 27 364
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
1.34e-44 125 462 25 364
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
5.25e-43 127 462 27 364
Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000272 0.999716 CS pos: 25-26. Pr: 0.9751

TMHMM  Annotations      help

There is no transmembrane helices in AO090103000218-T-p1.