Species | Globisporangium ultimum | |||||||||||
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Lineage | Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum | |||||||||||
CAZyme ID | PUG3_T000691-RA-p1 | |||||||||||
CAZy Family | AA17 | |||||||||||
CAZyme Description | Di-N-acetylchitobiase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.-:18 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH18 | 64 | 375 | 4.2e-37 | 0.8074324324324325 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
119354 | GH18_chitobiase | 2.49e-118 | 16 | 394 | 18 | 358 | Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase. |
214753 | Glyco_18 | 5.66e-31 | 64 | 376 | 30 | 333 | Glyco_18 domain. |
395573 | Glyco_hydro_18 | 7.75e-23 | 64 | 375 | 27 | 305 | Glycosyl hydrolases family 18. |
119353 | GH18_CFLE_spore_hydrolase | 2.94e-19 | 98 | 372 | 54 | 300 | Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis. |
119351 | GH18_chitolectin_chitotriosidase | 1.58e-17 | 159 | 381 | 137 | 345 | 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 |
---|---|---|---|---|---|
9.05e-144 | 14 | 395 | 464 | 834 | |
2.23e-130 | 1 | 397 | 19 | 384 | |
7.79e-129 | 13 | 397 | 2 | 355 | |
2.39e-111 | 7 | 394 | 17 | 381 | |
2.55e-85 | 63 | 394 | 56 | 375 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.79e-11 | 117 | 372 | 90 | 306 | Chain A, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168],3CZ8_B Chain B, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168] |
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9.00e-11 | 159 | 386 | 137 | 355 | The crystal structures of YKL-39 in the absence of chitooligosaccharides was solved to resolutions of 2.4 angstrom [Homo sapiens],4P8V_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc2) were solved to resolutions of 1.5 angstrom [Homo sapiens],4P8W_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc4) were solved to resolutions of 1.9 angstrom [Homo sapiens],4P8X_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc6) were solved to resolutions of 2.48 angstrom [Homo sapiens] |
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3.09e-10 | 119 | 381 | 98 | 354 | Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis] |
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9.73e-10 | 119 | 381 | 98 | 354 | Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis] |
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1.18e-09 | 159 | 386 | 131 | 349 | Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_B Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_C Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_D Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_E Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_F Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_G Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_H Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_I Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_J Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_K Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens],4AY1_L Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide binding properties [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.12e-86 | 7 | 394 | 5 | 363 | Di-N-acetylchitobiase OS=Rattus norvegicus OX=10116 GN=Ctbs PE=1 SV=1 |
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4.43e-85 | 63 | 394 | 43 | 362 | Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2 |
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1.24e-83 | 63 | 394 | 59 | 378 | Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1 |
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1.28e-58 | 62 | 397 | 43 | 373 | Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1 |
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1.64e-50 | 62 | 397 | 40 | 369 | Probable di-N-acetylchitobiase 1 OS=Dictyostelium discoideum OX=44689 GN=ctbs1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999758 | 0.000268 |
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