Species | Trichoderma reesei | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei | |||||||||||
CAZyme ID | TRIREDRAFT_119859-t26_1-p1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | glycoside hydrolase family 18, chitinase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.14:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 31 | 268 | 7.6e-25 | 0.6722972972972973 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
119356 | GH18_hevamine_XipI_class_III | 3.08e-97 | 30 | 315 | 1 | 280 | This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. |
395573 | Glyco_hydro_18 | 6.11e-16 | 31 | 256 | 1 | 203 | Glycosyl hydrolases family 18. |
119350 | GH18_chitinase_D-like | 5.58e-15 | 32 | 315 | 3 | 311 | GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus. |
119349 | GH18_chitinase-like | 1.24e-07 | 32 | 229 | 1 | 177 | The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model. |
226000 | Chi1 | 3.09e-04 | 104 | 298 | 91 | 302 | Chitinase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.78e-247 | 1 | 367 | 1 | 368 | |
7.73e-239 | 1 | 369 | 1 | 379 | |
6.00e-238 | 1 | 367 | 1 | 375 | |
3.53e-237 | 1 | 369 | 1 | 379 | |
1.99e-233 | 1 | 369 | 1 | 376 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.67e-46 | 30 | 307 | 1 | 264 | CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR [Hevea brasiliensis],1LLO_A Chain A, HEVAMINE [Hevea brasiliensis],2HVM_A Hevamine A At 1.8 Angstrom Resolution [Hevea brasiliensis] |
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1.54e-44 | 30 | 307 | 1 | 264 | Chain A, Hevamine A [Hevea brasiliensis] |
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3.02e-44 | 30 | 307 | 1 | 264 | Chain A, Hevamine A [Hevea brasiliensis] |
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1.16e-43 | 30 | 307 | 1 | 264 | Chain A, Hevamine A [Hevea brasiliensis],1KQZ_A Chain A, Hevamine A [Hevea brasiliensis] |
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8.32e-43 | 30 | 299 | 1 | 254 | cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.79e-148 | 1 | 317 | 1 | 317 | Endochitinase 3 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chi3 PE=3 SV=1 |
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3.17e-141 | 24 | 307 | 6 | 290 | Endochitinase 3 (Fragment) OS=Metarhizium anisopliae OX=5530 GN=chi3 PE=1 SV=1 |
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4.93e-46 | 29 | 307 | 26 | 290 | Hevamine-A OS=Hevea brasiliensis OX=3981 PE=1 SV=2 |
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6.30e-43 | 30 | 317 | 26 | 301 | Acidic endochitinase OS=Vitis vinifera OX=29760 GN=CHIT3 PE=2 SV=1 |
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1.55e-40 | 32 | 317 | 26 | 293 | Acidic endochitinase OS=Cicer arietinum OX=3827 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000301 | 0.999689 | CS pos: 26-27. Pr: 0.9573 |
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