CAZyme Information: ODM18520.1

Basic Information

• Species: Aspergillus cristatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus cristatus
• CAZyme ID: ODM18520.1
• CAZy Family: GH18
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1E3BC22]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
432	JXNT01000006|CGC6	47592.21	4.5512

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcristatusGZAAS20.1005	10344	N/A	0	10344

• Gene Location: location=JXNT01000006:1202729-1204149(-)

Full Sequence      

MMKHVLLGLLAAQTALSTRFVMYIDQYHTKDFPGKNLTEGITHAVMGFAKSDLFTSESTP
HYEPFEPVSTMRDRFSPDTKVLFAIGGWGDTEGFAAGAKDDTSRQQYAKNVAAVVEENGF
DGVDIDWEYPGGNGENYKDIPNEEKTGEIDAFPKLLEAIKKELPEGKILSIATPGKKGDM
IAYTDENGPKIAESVDMVNVMSYDLANRRNNVTKHHSSVEDSRETIKAYKGIGLPAGKLN
LGFAYYAKWFMTAKDADCKAHPLGCEMQELETPDGKDTGKSGVLTFEKGTMATPNKDDLK
ESTDGSCGYGTMTTCPEGQCCSQYGTCGTTDAHCQAGCLSDYGTCKGLSIIDSWRRADKD
GQLDEKAGGQYYFDDEEDLFWTWDTPEMIKRKFKDIVDEEKIGGVMAWSLGEDTLDFAHV
KAMQEGVKERSA

Enzyme Prediction     

EC	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	19	416	5.4e-54	0.9425675675675675

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	5.30e-81	19	413	1	307	Glycosyl hydrolases family 18.
214753	Glyco_18	1.30e-50	23	413	12	334	Glyco_18 domain.
119349	GH18_chitinase-like	4.21e-43	20	205	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.
119365	GH18_chitinase	5.09e-39	77	246	83	262	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.
119351	GH18_chitolectin_chitotriosidase	2.44e-34	42	417	29	343	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
BCR91516.1|CBM18|GH18	0.0	1	432	1	432
QRD94346.1|CBM18|GH18	1.24e-219	3	431	4	431
QMW33929.1|CBM18|GH18	1.24e-219	3	431	4	431
QMW45983.1|CBM18|GH18	1.24e-219	3	431	4	431
BAE63426.1|CBM18|GH18	1.76e-219	3	431	4	431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	4.18e-21	77	248	89	263	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	5.11e-21	77	248	108	282	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
1HKK_A	4.60e-17	36	286	28	282	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	4.64e-17	36	286	28	282	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	4.64e-17	36	286	28	282	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|Q9D7Q1|CHIT1_MOUSE	6.89e-19	9	286	13	303	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q13231|CHIT1_HUMAN	4.35e-16	36	286	49	303	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P32470|CHI1_APHAL	1.54e-15	12	283	39	330	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
sp|P11220|CHIT_STRPL	1.07e-14	18	428	248	610	Chitinase 63 OS=Streptomyces plicatus OX=1922 GN=chtA PE=1 SV=2
sp|E9QRF2|CHIB1_ASPFU	1.24e-14	20	250	52	303	Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001974	0.998000	CS pos: 17-18. Pr: 0.9585

TMHMM  Annotations     

There is no transmembrane helices in ODM18520.1.