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CAZyme Information: QRC96157.1

You are here: Home > Sequence: QRC96157.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRC96157.1
CAZy Family CE3
CAZyme Description chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
146 15708.62 5.6430
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 3 144 5.5e-16 0.3614864864864865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 3.19e-69 1 145 173 317
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 1.01e-14 5 113 176 275
Glyco_18 domain.
119351 GH18_chitolectin_chitotriosidase 1.47e-11 5 144 180 312
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 7.46e-10 4 144 166 278
Glycosyl hydrolases family 18.
119365 GH18_chitinase 2.21e-08 5 74 201 267
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
5.00e-105 1 146 1 146
8.97e-63 1 145 688 832
4.93e-61 1 146 471 616
4.52e-60 1 145 773 917
3.96e-59 1 145 774 918

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.48e-09 4 144 182 315
The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]
7.01e-09 5 132 185 306
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
7.01e-09 5 132 185 306
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
8.01e-08 5 144 177 306
Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
1.09e-07 5 144 177 306
Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution [Capra hircus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.92e-14 4 144 555 685
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
8.36e-11 1 144 201 331
Oviduct-specific glycoprotein OS=Papio anubis OX=9555 GN=OVGP1 PE=2 SV=2
6.88e-10 5 144 204 336
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
1.36e-09 1 144 201 331
Oviduct-specific glycoprotein OS=Homo sapiens OX=9606 GN=OVGP1 PE=2 SV=1
1.86e-09 1 144 201 331
Oviduct-specific glycoprotein OS=Mus musculus OX=10090 GN=Ovgp1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999164 0.000850

TMHMM  Annotations      help

There is no transmembrane helices in QRC96157.1.