CAZyme Information: ASPACDRAFT_2719-t33_1-p1

Basic Information

• Species: Aspergillus aculeatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus aculeatus
• CAZyme ID: ASPACDRAFT_2719-t33_1-p1
• CAZy Family: GH15|CBM20
• CAZyme Description: glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
563	KV878986|CGC3	60527.56	3.7131

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AaculeatusATCC16872	11165	690307	322	10843

• Gene Location: location=KV878986:876301-877989(-)

Full Sequence      

PQRRSSSTCSYIQVVSGDLCGTLADECGITLDDFYEYNSASDLCTTLAVGQYVCCSAGDL
PDFAPTVSANGTCYTYYVQWGDSCSALAAAYSMTVDDIESFNSETWGWYGCNDLQAGQSM
CLSNGTAPYPEPITNAVCGPQVPDTNFTGTDGPADWALLNPCPLNACCDVWGQCGTTPDY
CNDTSAATGAPGTAANNSNGCISNCGTTITNWANAPATYASVGYFEGYNVNRTCLRMNAY
TIDPAKYTHVHYGFGSIASDFSVASGPNPDQFKYFTELLGVKRVVSFGGWAFSTDPSTYM
IFREGVTEENRDTLAANIADFVTDNVLDGVDFDWEYPGEPDIPGIPAGSDEDGDNYLAFL
KVVREKLGSDKIISIAAPASYWYLKAFPIAEIADVVDYIIYMTYDLHGTWDLGDASAQSG
CPAGDCLFSHVNMTETMWSLAMITKAGVATDSLMVGVASYGRSFQMTTAGCTDSSCTWDA
AGAAGPCTDTAGYIANAEINEILASNPSATYSYETDSQTDILVYNETQWVGYMSNSTMSK
RHAYYQAYNFAGTTEWAIDLEEY

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	218	559	3.2e-54	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	221	561	2	345	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.
214753	Glyco_18	9.25e-61	222	560	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.13e-51	222	559	3	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	3.06e-43	221	465	1	267	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	1.80e-38	222	406	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS25711.1|CBM18|CBM50|GH18	1.08e-219	7	563	281	838
BCS25363.1|CBM18|GH18	1.01e-212	9	563	267	817
AEO70565.1|CBM18|CBM50|GH18	3.20e-208	9	563	303	859
QMW24763.1|CBM18|CBM50|GH18	1.40e-207	2	563	281	841
QRD89348.1|CBM18|CBM50|GH18	2.35e-207	2	563	281	841

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	1.81e-26	222	563	7	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
2YBT_A	5.14e-26	242	563	29	350	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]
3FXY_A	6.23e-26	242	563	25	346	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
6JM8_A	2.03e-25	222	563	7	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1HKK_A	3.35e-25	242	563	25	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	8.57e-111	8	559	192	710	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|Q95M17|CHIA_BOVIN	1.34e-30	213	563	16	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q6RY07|CHIA_RAT	1.75e-28	242	563	46	367	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	4.80e-27	242	563	46	367	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q9BZP6|CHIA_HUMAN	9.79e-26	217	563	20	367	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999995	0.000051

TMHMM  Annotations     

There is no transmembrane helices in ASPACDRAFT_2719-t33_1-p1.