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CAZyme Information: EEQ35624.1

You are here: Home > Sequence: EEQ35624.1

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 EEQ35624.1
CAZy Family GT57
CAZyme Description symbiotic chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1011 DS995708|CGC6 109973.61 6.2887
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

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 124 373 3.5e-49 0.777027027027027

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 4.16e-61 122 374 50 333
Glyco_18 domain.
119351 GH18_chitolectin_chitotriosidase 2.74e-60 122 374 54 340
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.
395573 Glyco_hydro_18 6.59e-58 119 373 43 305
Glycosyl hydrolases family 18.
119365 GH18_chitinase 1.02e-48 82 373 37 320
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.
119357 GH18_zymocin_alpha 2.25e-42 108 375 37 345
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.21e-181 25 530 38 624
1.62e-157 118 530 1 446
1.28e-146 2 567 8 698
1.12e-126 78 566 7 579
9.69e-99 6 528 8 603

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.30e-39 98 374 23 341
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]
3.61e-38 98 374 23 341
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]
8.73e-38 98 393 43 376
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]
1.22e-36 98 374 28 350
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
1.56e-36 98 374 28 350
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.39e-36 98 393 51 384
Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3
6.83e-35 98 374 22 334
Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1
1.08e-34 98 374 43 362
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.20e-34 97 421 42 403
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
1.97e-34 98 374 43 356
Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000224 0.999739 CS pos: 23-24. Pr: 0.9794

TMHMM  Annotations      help

There is no transmembrane helices in EEQ35624.1.