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CAZyme Information: EEQ33387.1

You are here: Home > Sequence: EEQ33387.1

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 EEQ33387.1
CAZy Family GT2
CAZyme Description chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1267 139403.49 5.4518
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 3.2.1.14:3 3.2.1.14:3 3.2.1.14:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 502 789 4.5e-35 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 6.69e-116 500 782 2 345
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 1.20e-40 500 830 2 307
Glyco_18 domain.
395573 Glyco_hydro_18 4.98e-39 502 782 4 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 8.01e-35 523 782 24 322
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.
119349 GH18_chitinase-like 4.93e-30 502 687 3 178
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.42e-301 23 1235 40 1476
3.40e-253 36 1240 43 1364
7.06e-248 11 1213 7 1328
3.28e-246 36 1235 33 1366
5.02e-246 36 1235 43 1351

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.03e-14 526 786 37 355
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]
1.08e-14 526 830 33 314
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis],5Y2A_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis]
1.14e-14 526 786 37 355
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]
1.08e-13 526 830 33 314
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 E2180L mutant in complex with PENTA-N-ACETYLCHITOOCTAOSE (NAG)5 [Ostrinia furnacalis],5Y2C_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 E2180L mutant in complex with PENTA-N-ACETYLCHITOOCTAOSE (NAG)5 [Ostrinia furnacalis]
1.66e-13 562 701 159 298
Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.29e-80 166 786 89 716
Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
2.09e-12 526 701 52 228
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
7.01e-12 523 701 62 255
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
1.64e-11 556 716 118 271
Endochitinase 1 OS=Metarhizium anisopliae OX=5530 GN=chit1 PE=1 SV=1
3.83e-11 488 701 29 256
Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000328 0.999654 CS pos: 19-20. Pr: 0.9740

TMHMM  Annotations      help

There is no transmembrane helices in EEQ33387.1.