CAZyme Information: ODM14596.1

Basic Information

• Species: Aspergillus cristatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus cristatus
• CAZyme ID: ODM14596.1
• CAZy Family: AA3
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1E3B2A9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
455		51046.33	4.4158

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=JXNT01000023:43300-44983(+)

Full Sequence      

MIPQSIPQSVYSHIYFAFGSIDPGTFEVIPTSEEDEVLYPQLQALQSRDLSQELWLSIGG
WDFSDYDVPTATTFSDLGFTGVDIDWEYPAAGDRNGRAEDYNNFPGFLANLKKVLDEYKF
GLSVTLPTSYWYLRHFDLVSIEPSVDWFNFMSYDLHGTWDIGNQWTGAYLDAHTNLTEIE
SALDLLWRNNITASKFLISAGVLYNNEIKQIISENDLNPTLYKDAAVKSITRNNDQWVSY
DDQDTWKLKQSHILQRVAAALGNEINLDICTGLTSAVFSEKSTSDTSSSEKGQDQCCRFI
NCGEVCPSGFTEDITRPSVVSRGYMPDYRAQYRYSRTYAGGSRNTENMHDYDARTQALSS
NIGGNNRWYVGIDRSDAINTLETTSRPTRASGYNYRQSTFSVSNLQYLFPTLSNYGGDGF
PTPASLNARGIFNPKLGHSMRIGCLAAPDLSNADP

Enzyme Prediction     

No EC number prediction in ODM14596.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	5	252	2.9e-29	0.7905405405405406

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	2.25e-36	1	245	18	321	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.
395573	Glyco_hydro_18	2.37e-34	2	249	14	287	Glycosyl hydrolases family 18.
119365	GH18_chitinase	5.76e-32	3	256	18	309	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.
119349	GH18_chitinase-like	6.82e-29	2	155	15	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.
214753	Glyco_18	9.99e-29	3	249	18	314	Glyco_18 domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07677.1|CBM18|GH18	1.71e-133	1	311	133	519
QKD59080.1|CBM18|GH18	1.46e-114	1	312	136	515
QKD61252.1|CBM18|GH18	1.46e-114	1	312	136	515
CZS74851.1|CBM18|GH18	6.03e-113	1	312	164	543
CEF84382.1|CBM18|GH18	6.36e-113	1	312	136	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GZU_A	1.06e-17	4	205	43	284	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
5GZT_B	1.18e-17	4	205	294	535	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
1WNO_A	1.70e-15	3	198	23	256	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]
1W9P_A	2.08e-15	3	198	61	294	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]
1D2K_A	5.51e-13	3	160	21	211	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	2.66e-19	1	218	398	625	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|E9QRF2|CHIB1_ASPFU	1.07e-14	3	198	61	294	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	1.07e-14	3	198	61	294	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
sp|Q92222|CHIB_EMEND	5.17e-13	3	208	22	250	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
sp|G5EAZ3|CHIB1_EMENI	5.17e-13	3	208	22	250	Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ODM14596.1.