CAZyme Information: PWY85600.1

Basic Information

• Species: Aspergillus eucalypticola
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
• CAZyme ID: PWY85600.1
• CAZy Family: GT69
• CAZyme Description: glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
786	MSFU01000001|CGC10	85012.40	3.8926

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AeucalypticolaCBS122712	12207	1448314	274	11933

• Gene Location: location=MSFU01000001:1461058-1463499(+)

Full Sequence      

CPAPCSSTDPADWFVYPDLERLAQCNESMLLDFNIYNTVTDPQHHSTIYTCTTPGDLASW
GPSSTNSSDSGSSSPVTYEVGIWKASSPPGSSQLLALLRDMHSYLIANPHKGELFGYSNR
VSVGVYLGGSLQLTPNVDFALNEMISLSQNSTYDRAILQYCGSNANNTLGVAVSTNGDIT
TVQQYIQSWSKADCISDYDSHSSGTTTLWTSQTGLRNSTGAFTTITSNTTTSSHSSCSYI
QVVSGDLCATLVSECGITAAEFYQYNTASDLCSTLEVGQYVCCSSGGLPDFSPSAYSNGT
CYTYTVQSGDTCSALAQTYSLTVAEIDSYNNDTWGWYGCDDLQAGTNICLSTGNAPYPAA
ITNAVCGPQVPGTNFTDAPTSFYWAQLNPCPLNACCDVWGQCGTTPLYCNDTRASTGAPG
TAAAGSNGCIYNCGTNITNYAEEPSGYDVIGYLEASSVNRTCLRWQASDVNTTKYTHVNF
GFGNIASDFSINVDGMESDFNLFLKLVGTKRILSFGGWDFSTSSSTYMIFREGTAAANRE
TFATNVANFITEKELDGVDFDWEYPGEPDISGIPAGGSDEGENYLEFLKVLRALVANDTI
ISVTAPSSYWYLKAFPIAEMAEVVDYINYMTYDLHGIWDLGNEYSQWGCSDGDCLFSHVN
MTETMWALAMITKAGVATKDIRVGVSSYGRSFHMTTAGCYESWCTYDTAGAAGPCTDTAG
YIAEAEMEEILASDTTTQTYSTYDTDILVYNETQWVGYMNSTTRASRMAYYEQFNFGGTA
EWAIDL

Enzyme Prediction     

EC	-	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	447	785	1.7e-47	0.9290540540540541

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	1.28e-170	450	786	3	344	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	5.00e-53	449	786	2	333	Glyco_18 domain.
395573	Glyco_hydro_18	2.03e-45	449	785	2	305	Glycosyl hydrolases family 18.
119349	GH18_chitinase-like	1.69e-36	449	634	1	178	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.
119351	GH18_chitolectin_chitotriosidase	3.07e-36	476	786	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS25711.1|CBM18|CBM50|GH18	7.50e-232	1	786	40	835
QQK44152.1|CBM18|CBM50|GH18	5.99e-230	1	786	57	873
UKZ79393.1|CBM18|CBM50|GH18	6.43e-224	1	786	82	886
UKZ53593.1|CBM18|CBM50|GH18	4.03e-223	1	786	82	886
BCS25363.1|CBM18|GH18	4.07e-219	1	786	30	814

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	4.72e-28	449	786	4	341	Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
5WVF_A	4.95e-27	449	786	4	341	Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
2YBT_A	4.80e-25	464	786	23	347	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
3FXY_A	5.86e-25	464	786	19	343	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
5WUP_A	2.11e-24	442	786	88	437	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	4.74e-108	237	785	193	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
sp|Q95M17|CHIA_BOVIN	7.00e-26	430	786	5	364	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	4.07e-25	441	786	16	364	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	5.45e-25	445	786	20	364	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q9BZP6|CHIA_HUMAN	3.32e-22	510	786	91	364	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000001

TMHMM  Annotations     

There is no transmembrane helices in PWY85600.1.