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CAZyme Information: THC90472.1

You are here: Home > Sequence: THC90472.1

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 Aspergillus tanneri
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
CAZyme ID THC90472.1
CAZy Family CE1
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A4S3J6S5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1200 136180.20 6.3518
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AtanneriNIH1004 13590 N/A 33 13557
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 138 481 9.5e-66 0.9493243243243243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 1.89e-79 139 477 1 334
Glyco_18 domain.
119351 GH18_chitolectin_chitotriosidase 1.23e-74 140 484 1 344
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.
119357 GH18_zymocin_alpha 3.99e-74 141 474 3 342
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.
395573 Glyco_hydro_18 2.31e-72 139 477 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 4.81e-64 140 477 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
4.38e-270 23 1190 18 1207
1.14e-260 10 1163 13 1218
2.34e-253 1 1189 5 1256
2.93e-252 11 1080 16 1107
2.37e-248 22 1187 18 1214

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.54e-44 139 477 3 342
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]
3.92e-43 139 477 3 342
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]
3.07e-38 139 484 2 348
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
3.14e-38 139 484 2 348
Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
3.14e-38 139 484 2 348
Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.19e-36 139 484 23 369
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.45e-35 140 483 24 371
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
2.89e-35 139 483 21 361
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
1.16e-34 140 483 24 371
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
1.54e-34 139 477 31 366
Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000201 0.999785 CS pos: 23-24. Pr: 0.9805

TMHMM  Annotations      download full data without filtering help

Start End
7 24