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CAZyme Information: PUG3_T000691-RA-p1

You are here: Home > Sequence: PUG3_T000691-RA-p1

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 Globisporangium ultimum
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
CAZyme ID PUG3_T000691-RA-p1
CAZy Family AA17
CAZyme Description Di-N-acetylchitobiase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
399 45061.92 4.9557
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GultimumBR650 14086 1223559 0 14086
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-:18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 64 375 4.2e-37 0.8074324324324325

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]
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]
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]
9.73e-10 119 381 98 354
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
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]

Swiss-Prot Hits      download full data without filtering help

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
4.43e-85 63 394 43 362
Di-N-acetylchitobiase OS=Mus musculus OX=10090 GN=Ctbs PE=1 SV=2
1.24e-83 63 394 59 378
Di-N-acetylchitobiase OS=Homo sapiens OX=9606 GN=CTBS PE=1 SV=1
1.28e-58 62 397 43 373
Probable di-N-acetylchitobiase 2 OS=Dictyostelium discoideum OX=44689 GN=ctbs2 PE=3 SV=1
1.64e-50 62 397 40 369
Probable di-N-acetylchitobiase 1 OS=Dictyostelium discoideum OX=44689 GN=ctbs1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999758 0.000268

TMHMM  Annotations      help

There is no transmembrane helices in PUG3_T000691-RA-p1.