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CAZyme Information: GBF66810.1

You are here: Home > Sequence: GBF66810.1

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 Trichophyton mentagrophytes
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
CAZyme ID GBF66810.1
CAZy Family GT90
CAZyme Description killer toxin subunits alpha/beta
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
483 BFBS01016519|CGC2 52284.38 5.9951
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789 7958 N/A 98 7860
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:3

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 9.41e-54 251 455 2 343
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 8.11e-09 324 455 204 332
Glyco_18 domain.
119351 GH18_chitolectin_chitotriosidase 1.66e-06 335 461 228 345
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 6.56e-06 318 455 192 305
Glycosyl hydrolases family 18.
197609 LysM 1.36e-04 114 157 1 40
Lysin motif.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.52e-138 1 482 201 879
2.85e-137 1 482 209 885
3.17e-135 1 461 204 852
1.32e-133 1 482 206 881
1.32e-133 1 482 206 881

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.66e-08 337 459 231 342
Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_B Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_C Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_D Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_E Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_F Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_G Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_H Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_I Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_J Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_K Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_L Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens]
2.30e-08 337 461 238 355
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]
2.40e-08 337 461 238 355
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]
1.65e-07 337 459 237 348
The crystal structures of YKL-39 in the absence of chitooligosaccharides was solved to resolutions of 2.4 angstrom [Homo sapiens],4P8V_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc2) were solved to resolutions of 1.5 angstrom [Homo sapiens],4P8W_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc4) were solved to resolutions of 1.9 angstrom [Homo sapiens],4P8X_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc6) were solved to resolutions of 2.48 angstrom [Homo sapiens]
4.79e-06 317 459 206 337
Crystal structure of a 40 KDa protective signalling protein from Bovine (SPC-40) at 2.1 A resolution [Bos taurus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.51e-33 39 336 173 464
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
9.31e-08 337 459 256 367
Chitinase-3-like protein 2 OS=Homo sapiens OX=9606 GN=CHI3L2 PE=1 SV=1
6.72e-06 337 461 1197 1314
Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000086 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in GBF66810.1.