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CAZyme Information: EEQ29481.1

You are here: Home > Sequence: EEQ29481.1

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 Microsporum canis
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Microsporum; Microsporum canis
CAZyme ID EEQ29481.1
CAZy Family CE9
CAZyme Description symbiotic chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1176 126526.43 5.8619
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_McanisCBS113480 8847 554155 82 8765
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 45 349 2.8e-56 0.9324324324324325

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119351 GH18_chitolectin_chitotriosidase 6.07e-74 75 350 29 340
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.
214753 Glyco_18 1.14e-73 49 350 3 333
Glyco_18 domain.
395573 Glyco_hydro_18 3.62e-69 47 349 1 305
Glycosyl hydrolases family 18.
119357 GH18_zymocin_alpha 2.22e-59 49 351 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.
119365 GH18_chitinase 5.73e-55 49 349 2 320
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
1.38e-234 23 507 109 628
9.61e-215 93 1135 1 1004
4.88e-155 24 483 101 599
2.68e-128 76 502 24 510
1.45e-107 14 501 105 603

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.81e-45 47 350 23 357
Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_B Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_C Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_D Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_E Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_F Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus]
3.81e-43 51 370 7 371
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]
4.16e-42 47 350 2 334
Crystal structure of a 40 kDa signalling protein (SPC-40) secreted during involution [Bos taurus]
4.21e-42 51 370 7 371
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]
1.06e-41 47 350 2 335
Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_B Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_C Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_D Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJW_A Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJW_B Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJX_A Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_B Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_C Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_D Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1NWR_A Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_B Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_C Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_D Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWS_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWT_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWU_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],7CJ2_A Chain A, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens],7CJ2_B Chain B, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.26e-44 47 350 21 354
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
9.44e-44 47 350 31 365
Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3
8.86e-41 47 350 23 356
Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2
1.33e-40 47 350 2 334
Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1
1.60e-40 47 350 50 383
Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000030 0.000012

TMHMM  Annotations      help

There is no transmembrane helices in EEQ29481.1.