CAZyme Information: ASPFODRAFT_121506-t33_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: ASPFODRAFT_121506-t33_1-p1
• CAZy Family: AA1
• CAZyme Description: glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
181	KV878236|CGC21	20773.29	4.6552

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisCBS106.47	13784	1137211	282	13502

• Gene Location: location=KV878236:22804-23408(-)

Full Sequence      

MSHDRRIGYYELFKIHKGCHTIEPESLIIEPFTHINLAFVNFGDDFKLEDEYGDIVDRVS
FSKFTHPGLRVNIAVGGWMLNDAPTQHLWTQMARSYENRQIIINSVVKYLKDYYLDGIDI
DWEYPSASDKGGEPQDAANFVTLLGELREAFDRDNPGWEISPTLPTSYSYLRGFDPAGMA
K

Enzyme Prediction     

No EC number prediction in ASPFODRAFT_121506-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	5	174	7.2e-27	0.44932432432432434

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	1.48e-31	29	161	23	157	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.
119349	GH18_chitinase-like	2.52e-30	7	171	2	155	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.
214753	Glyco_18	3.46e-30	5	171	1	162	Glyco_18 domain.
119357	GH18_zymocin_alpha	2.73e-29	5	181	1	175	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	8.72e-29	7	181	2	199	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS09174.1|GH18	1.40e-137	1	181	1	181
BCR96672.1|GH18	1.40e-137	1	181	1	181
EAA66616.1|CBM18|GH18	9.02e-87	1	181	138	304
BCS25298.1|CBM18|GH18	2.49e-82	1	175	138	312
AIT18875.1|GH18	2.13e-51	6	175	86	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL1_A	9.82e-26	2	174	5	182	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]
3W4R_A	2.57e-25	2	174	23	200	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
3WKZ_A	2.61e-25	2	174	5	182	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3WL0_A	6.95e-25	2	174	5	182	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
2YBT_A	1.80e-19	33	154	35	152	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36362|CHIT_MANSE	1.61e-23	2	174	21	198	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q6RY07|CHIA_RAT	3.96e-19	18	154	37	169	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	7.39e-19	18	154	37	169	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9BZP6|CHIA_HUMAN	3.53e-18	33	154	52	169	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q95M17|CHIA_BOVIN	3.08e-17	18	154	37	169	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPFODRAFT_121506-t33_1-p1.