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CAZyme Information: ASPZODRAFT_20739-t33_1-p1

You are here: Home > Sequence: ASPZODRAFT_20739-t33_1-p1

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 Penicilliopsis zonata
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
CAZyme ID ASPZODRAFT_20739-t33_1-p1
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1071 KV878367|CGC1 117234.13 4.7353
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PzonataCBS506.65 10027 1073090 158 9869
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ASPZODRAFT_20739-t33_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 83 454 6.8e-62 0.956081081081081

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 6.08e-86 84 448 1 334
Glyco_18 domain.
119357 GH18_zymocin_alpha 1.79e-83 84 448 1 345
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.
119351 GH18_chitolectin_chitotriosidase 3.75e-73 85 450 1 343
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 3.57e-67 84 448 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 3.40e-65 85 448 1 322
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 3 1044 75 1130
0.0 3 1044 75 1130
0.0 70 1059 20 1012
2.27e-269 4 1025 7 1018
1.17e-257 3 1027 58 1042

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.40e-48 85 450 6 352
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
2.46e-47 84 450 94 440
Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
3.88e-47 84 536 3 417
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]
7.34e-47 85 450 6 352
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
2.74e-46 84 450 94 440
Crystal structure of a mutant insect group III chitinase (CAD1-E217L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVB_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)6 (CAD1-E217L-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.48e-42 81 450 20 365
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.78e-41 85 450 24 367
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
3.24e-41 85 450 24 367
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
6.74e-41 81 450 20 363
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
1.92e-40 84 450 23 367
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999052 0.000986

TMHMM  Annotations      help

There is no transmembrane helices in ASPZODRAFT_20739-t33_1-p1.