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CAZyme Information: M747DRAFT_297598-t43_1-p1
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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 niger | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
| CAZyme ID | M747DRAFT_297598-t43_1-p1 | |||||||||||
| CAZy Family | GH2 | |||||||||||
| CAZyme Description | class V chitinase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH18 | 32 | 353 | 6.4e-70 | 0.9391891891891891 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 214753 | Glyco_18 | 4.02e-92 | 32 | 349 | 3 | 334 | Glyco_18 domain. |
| 119365 | GH18_chitinase | 1.44e-89 | 31 | 349 | 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. |
| 395573 | Glyco_hydro_18 | 2.39e-81 | 32 | 349 | 3 | 307 | Glycosyl hydrolases family 18. |
| 119351 | GH18_chitolectin_chitotriosidase | 1.39e-69 | 34 | 346 | 4 | 338 | 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. |
| 225862 | ChiA | 3.66e-66 | 13 | 366 | 21 | 434 | Chitinase, GH18 family [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 5.67e-280 | 1 | 367 | 1 | 367 | |
| 5.67e-280 | 1 | 367 | 1 | 367 | |
| 3.16e-270 | 1 | 354 | 1 | 354 | |
| 2.60e-240 | 7 | 367 | 7 | 369 | |
| 2.60e-240 | 7 | 367 | 7 | 369 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.41e-70 | 9 | 364 | 4 | 376 | Crystal structure of Aspergillus niger chitinase B [Aspergillus niger] |
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| 2.95e-68 | 29 | 364 | 3 | 363 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL4_A Chain A, Chitinase 1 [Coccidioides immitis],1LL4_B Chain B, Chitinase 1 [Coccidioides immitis],1LL4_C Chain C, Chitinase 1 [Coccidioides immitis],1LL4_D Chain D, Chitinase 1 [Coccidioides immitis] |
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| 8.26e-68 | 29 | 364 | 3 | 363 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis] |
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| 1.64e-67 | 29 | 364 | 3 | 363 | Chain A, CHITINASE 1 [Coccidioides immitis],1LL6_B Chain B, CHITINASE 1 [Coccidioides immitis],1LL6_C Chain C, CHITINASE 1 [Coccidioides immitis],1LL6_D Chain D, CHITINASE 1 [Coccidioides immitis] |
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| 7.68e-66 | 29 | 364 | 5 | 366 | Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.22e-68 | 29 | 360 | 4 | 358 | Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1 |
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| 3.22e-68 | 29 | 360 | 4 | 358 | Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3 |
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| 1.38e-67 | 19 | 364 | 22 | 398 | Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1 |
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| 3.84e-67 | 29 | 364 | 38 | 398 | Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1 |
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| 7.60e-67 | 19 | 364 | 22 | 398 | Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.998658 | 0.001350 |