Species | Scedosporium apiospermum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum | |||||||||||
CAZyme ID | SAPIO_CDS4086-t41_1-p1 | |||||||||||
CAZy Family | GH125 | |||||||||||
CAZyme Description | Mannan endo-1,4-beta-mannosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.14:2 | 3.2.1.78:33 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 615 | 885 | 3.8e-84 | 0.9930795847750865 |
GH18 | 15 | 348 | 1.5e-59 | 0.956081081081081 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
214753 | Glyco_18 | 2.04e-66 | 17 | 343 | 1 | 334 | Glyco_18 domain. |
395573 | Glyco_hydro_18 | 5.63e-61 | 17 | 343 | 1 | 307 | Glycosyl hydrolases family 18. |
119357 | GH18_zymocin_alpha | 1.29e-56 | 19 | 340 | 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. |
119365 | GH18_chitinase | 6.93e-56 | 18 | 343 | 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. |
119351 | GH18_chitolectin_chitotriosidase | 2.30e-54 | 36 | 348 | 19 | 346 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.28e-184 | 571 | 919 | 17 | 367 | |
6.73e-169 | 585 | 921 | 29 | 368 | |
6.90e-160 | 580 | 919 | 117 | 459 | |
3.29e-159 | 584 | 921 | 13 | 353 | |
6.02e-159 | 584 | 921 | 30 | 370 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.86e-160 | 584 | 921 | 16 | 356 | Chain A, Gh5 Endo-beta-1,4-mannanase [Podospora anserina] |
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2.87e-151 | 583 | 921 | 2 | 344 | The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger],3WH9_B The ligand-free structure of ManBK from Aspergillus niger BK01 [Aspergillus niger] |
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2.18e-150 | 581 | 919 | 2 | 343 | Chain A, ENDO-1,4-B-D-MANNANASE [Trichoderma reesei],1QNP_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNQ_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNR_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei],1QNS_A Chain A, Endo-1,4-b-d-mannanase [Trichoderma reesei] |
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3.60e-141 | 583 | 919 | 3 | 342 | Crtstal structure of glycoside hydrolase family 5 beta-mannanase from Talaromyces trachyspermus [Talaromyces trachyspermus] |
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5.42e-68 | 581 | 919 | 2 | 356 | Crystal Structure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.07e-159 | 584 | 921 | 30 | 370 | Mannan endo-1,4-beta-mannosidase A OS=Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OX=515849 GN=Pa_6_490 PE=1 SV=1 |
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4.19e-157 | 583 | 921 | 43 | 384 | Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=manA PE=3 SV=1 |
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6.58e-156 | 583 | 923 | 43 | 386 | Probable mannan endo-1,4-beta-mannosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=manA PE=3 SV=2 |
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5.74e-153 | 570 | 921 | 13 | 368 | Probable mannan endo-1,4-beta-mannosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=manA PE=3 SV=1 |
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9.19e-152 | 580 | 919 | 87 | 430 | Probable mannan endo-1,4-beta-mannosidase F OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=manF PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000091 | 0.000000 |
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