CAZyme Information: EAW20654.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW20654.1
• CAZy Family: GH38
• CAZyme Description: glycosyl hydrolase, family 18, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
191		21916.98	6.8447

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

• Gene Location: location=DS027693:706693-707553(+)

Full Sequence      

MRLFQSFCLNITSLHFNCASLFLRVVGYYEFWSSRRGCNTVWPEQIKLGVYSHINFAFAT
IHPKTYEVLPANEWDVPLYKHPADLKQYDPNLKVMIVLGGWTFNDPGPAATLFFDLAASE
EKQKKFVKSVSFMSTCDFDGVNLDWEYPEASDWSGRPADYDNFPRFTVNLKSSLDKTPGR
SKLSITLPALY

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	24	189	8e-25	0.43243243243243246

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	8.49e-34	24	189	1	157	Glyco_18 domain.
395573	Glyco_hydro_18	4.00e-33	24	191	1	151	Glycosyl hydrolases family 18.
119349	GH18_chitinase-like	3.11e-32	25	191	1	152	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	1.09e-30	25	189	1	162	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.
119365	GH18_chitinase	2.07e-27	25	189	1	184	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
CZS83161.1|CBM18|GH18	6.28e-66	24	191	122	290
BCS04193.1|GH18	2.53e-64	24	191	77	245
BCS15787.1|GH18	2.56e-64	24	191	89	257
ATY64693.1|CBM18|GH18	6.81e-64	24	189	141	306
EAA67103.1|CBM18|GH18	1.55e-62	24	191	110	278

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	5.66e-18	24	191	3	164	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	6.74e-17	24	191	3	164	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]
1HKK_A	5.94e-16	24	189	2	165	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	5.97e-16	24	189	2	165	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1HKI_A	5.97e-16	24	189	2	165	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9WTV1|CH3L1_RAT	1.29e-15	24	186	21	173	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
sp|Q13231|CHIT1_HUMAN	4.13e-15	24	189	23	186	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P36222|CH3L1_HUMAN	1.17e-14	18	186	18	175	Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2
sp|Q5RBP6|CH3L1_PONAB	1.27e-14	18	152	45	173	Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1
sp|P36362|CHIT_MANSE	1.52e-14	24	188	24	188	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.996742	0.003280

TMHMM  Annotations     

There is no transmembrane helices in EAW20654.1.