Species | Fusarium circinatum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum | |||||||||||
CAZyme ID | KAF5682499.1 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | killer toxin subunits alpha beta | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.14:3 | 3.2.1.14:3 | 3.2.1.14:3 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 517 | 871 | 2.8e-54 | 0.918918918918919 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
119357 | GH18_zymocin_alpha | 0.0 | 516 | 873 | 2 | 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. |
214753 | Glyco_18 | 6.33e-61 | 517 | 872 | 3 | 333 | Glyco_18 domain. |
395573 | Glyco_hydro_18 | 4.49e-52 | 517 | 871 | 3 | 305 | Glycosyl hydrolases family 18. |
119351 | GH18_chitolectin_chitotriosidase | 1.22e-45 | 545 | 872 | 29 | 340 | 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. |
119365 | GH18_chitinase | 1.64e-41 | 544 | 761 | 26 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 880 | 1 | 880 | |
0.0 | 1 | 880 | 1 | 880 | |
0.0 | 1 | 880 | 1 | 881 | |
0.0 | 1 | 880 | 4 | 883 | |
0.0 | 1 | 880 | 1 | 830 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.32e-28 | 545 | 873 | 34 | 350 | Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis] |
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7.92e-27 | 545 | 873 | 34 | 350 | Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis] |
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3.87e-25 | 545 | 873 | 37 | 359 | Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis] |
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9.40e-25 | 545 | 873 | 37 | 359 | Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis] |
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1.90e-24 | 545 | 873 | 55 | 377 | Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.59e-94 | 331 | 871 | 218 | 710 | 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 |
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8.24e-27 | 545 | 873 | 52 | 365 | Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1 |
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5.53e-24 | 545 | 873 | 53 | 375 | Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1 |
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4.84e-23 | 545 | 873 | 52 | 363 | Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1 |
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1.27e-22 | 545 | 873 | 52 | 365 | Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000197 | 0.999778 | CS pos: 20-21. Pr: 0.9800 |
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