CAZyme Information: ASPFODRAFT_126901-t33_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: ASPFODRAFT_126901-t33_1-p1
• CAZy Family: AA3
• CAZyme Description: glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
447	KV878238|CGC10	48943.09	4.9687

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=KV878238:2008694-2010462(+)

Full Sequence      

MAFSRLIHCLVLFIVVLILSARYLWNDAAVLPLQPNSAPTTDTNATIPAMSSGLKSVAYF
VNWAIYGRNYNPQDIPADKLTHVLYAFANVRPDTGEVYLSDTWSDIEKHYPTDSWNDVGT
NVYGCVKQLFLLKQQNRKLKVLLSIGGWTYSPNFAQAASTDAGRTKFAETATKLVTDLGF
DGIDIDWEYPKDDTEAQNMVLLLQKCRETLDATAGANRKFLLTIACPAGPANYTKLKLSQ
MTPYLDFYNLMAYDYAGSWDTVAGHQANLYPSADKPASTPFSTNEAVNYYIQKGGVPSSK
IILGMPLYGRAFTNTDGPGTAFSGVGEGSWEQGVWDYKALPRTGATEHVDASLGASWSYD
PTARTMVSYDTVAVGEMKLDYITKLQLGGGMWWETSGDKGGKTANKADGSLIGTFVEGIG
GVSALDQSQNVLSYPESKYDNLRNAFQ

Enzyme Prediction     

EC	3.2.1.14:25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	55	406	5.3e-82	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119365	GH18_chitinase	1.01e-131	56	398	1	322	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.
214753	Glyco_18	2.78e-125	55	398	1	334	Glyco_18 domain.
395573	Glyco_hydro_18	1.77e-91	55	398	1	307	Glycosyl hydrolases family 18.
225862	ChiA	7.71e-89	55	421	39	438	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351	GH18_chitolectin_chitotriosidase	1.80e-76	57	393	2	336	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
BCS06167.1|GH18	0.0	1	447	1	447
BCR93532.1|GH18	1.56e-312	33	447	1	415
CAK44246.1|GH18|3.2.1.14	8.27e-308	33	447	1	415
QRD82563.1|GH18	5.98e-244	4	446	4	435
QMW40166.1|GH18	5.98e-244	4	446	4	435

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9P_A	2.99e-185	15	447	11	432	Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9P_B Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9U_A Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9U_B Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9V_A Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],1W9V_B Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],2A3A_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3A_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3B_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3B_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3C_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3C_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3E_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2A3E_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2IUZ_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],2IUZ_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],3CH9_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CH9_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CHC_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHC_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHD_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHD_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHE_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHE_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHF_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus],3CHF_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus]
1WNO_A	6.32e-185	51	447	2	394	Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus]
1D2K_A	1.32e-183	53	445	2	389	Chain A, CHITINASE 1 [Coccidioides immitis],1LL4_A Chain A, Chitinase 1 [Coccidioides immitis],1LL4_B Chain B, Chitinase 1 [Coccidioides immitis],1LL4_C Chain C, Chitinase 1 [Coccidioides immitis],1LL4_D Chain D, Chitinase 1 [Coccidioides immitis]
6IGY_A	2.51e-183	51	446	13	403	Crystal structure of Aspergillus niger chitinase B [Aspergillus niger]
1LL7_A	3.77e-183	53	445	2	389	Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92222|CHIB_EMEND	3.38e-227	52	446	2	395	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
sp|G5EAZ3|CHIB1_EMENI	3.38e-227	52	446	2	395	Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1
sp|E9QRF2|CHIB1_ASPFU	1.54e-184	15	447	11	432	Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
sp|Q873X9|CHIB1_ASPFM	1.54e-184	15	447	11	432	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
sp|Q1E3R8|CHI1_COCIM	5.04e-184	27	445	16	424	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.814719	0.185280

TMHMM  Annotations     

Start	End
7	25