CAZyme Information: ASPNIDRAFT2_1086727-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ASPNIDRAFT2_1086727-t41_1-p1
• CAZy Family: AA3
• CAZyme Description: Carbohydrate-Binding Module Family 18 / Glycoside Hydrolase Family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1747		194365.33	4.5674

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerATCC1015	11910	380704	6	11904

• Gene Location: location=ACJE01000008.1:1927044-1932956(-)

Full Sequence      

MNSLTWPLLFICLILLQLPSAIAQGPGEPGGTCTDSIPCYQGCCSKDYSCGFTDAHCGTG
CRSNCNATAECGEFAAPGNSDCPINVCCSSFGYCGVTSEFCGNGCQKNSNGGGCGQPNRP
KCSENTDAMTYDRRIGYYELFNIHKGCNVIEPESLIIEPFTHINLAFVNFDEYGDIVDRV
SFLKFTHPGLRVNIAVGGWTFSDAPTQHLWTQMARSYENRQTFINSVVKYLKDYHLDGID
IDWEYPSASDRGGEPQDAANFVTLLGELREAFDRENPGWEISATLPTSYWYLRGFDPAGM
AKYVDYFNLMSYDLHGMWDQDITWTGPYLKGHTNITEIDLGLDLLWRNDVDPSKVVFGFA
FYGRSFTMADPNCYQPNGKCEFSDGGIPGSCSDTSGILTYAEVASRNNSLDVHTFYDPET
TVKYNVYKGTQWISYDDEQSFFDKKKFISSRCLSGWMIWAIDQDDGDFDALAGVIGEDLS
VMQMEGGGLSGDAANALADAFAAYTGQNCFVTPRCTDGSSGEKNPDQVCPSGYMSVSTAH
NPLQAGNKELHGDCSEGWYRHICCPEDAMPKNCEWNGAPERSEFGCDGKCGKNQFKLNQD
TALDAEGEGQCFIGERYLCCDSAAMFSDCKWTDCQGPLLPYTPGECPADNDALTFRWDKP
DGKPWCSDTYVSSVDGSVGSPLHDRFKSELCCPSDHSFSVSGCAWTNTITEADMKDDDWA
EHITDLVCKPRPCSPGKVKVAGALDPPPAMGAGSKSEINCDGVTIPPGSDPEWSFCCDPP
SRYDKNWPVDPKYLWEKYYNDPKKSDVVWEYSDEYQNNNMDSEPSTEEDGSDAYGFVMLD
GPDGSIDNDFATSHTVVRRSREIPRVKRSVLTTNQTLMDTVFDHAEETFHVYCNYPAESH
ECERVFIDGAEDTIIRLPDHVGEGPFARIVSMKAAHDEYQLPDHHLEHRSLERNTNPVYE
VKIDYNFHLIKLKRDDEPVNIRVDYTNLMGYWDEMTNSPAIRTKRGLGEEGLTEDEWRSR
VQRAIVRHSNIEKRNENIHVKTPMEFTGSHLDKRWWGAFKAWLQKLTTVTKSSLGVIELG
FSKTINLFWAQWGCPGQTFSANLRMDLEADLVMDATYAYYLSATFIPPGKPETFAYFGMN
PTAYLGLHIEGNAQMQTTTDRKKIIDTLSYPGLAVKGIAAVGPTLDIYGEATAGAQLFFG
KAEVYWPQNDDAKDKYETLLGLQSDVQAPAPGSVEPVFEAGVALDAQLDIIVTPEAHVGI
KIGGGKLVGGATLMDAQLTGYVIGDLSFQAHGDYDTTGNEFNYRFGVYLFYNLGYKATAQ
ILNFIDWALAPRMAYDPRKTFKLYEKKGSIPMSSSAKSKREATIDGPLHQDLVEVGSLTN
GSISTYLDSASGLSRRGDEMDIDGPNAPEFTQNLKCPPGTSGDVQLPEIRFNCDFLNDFI
EQSKNGKMDAITGLCTPVLNIPDNKRQKLFTFSNDEARKDARYNAQCPAGTCKQVTTDLK
THQANKNLELQCDEFPWKSSEQGGDYLASDARTGTCVASYQNNWHGQCLRMIGDMESNWA
KLEPERKDGDDRGDYWLSWRSGVWTKPGQHGPQGSQYEQRLKEYPEKQPMPDGVPTRSND
KISWVFKRDYEVSFIRQDPSTIDGSTWWGATSHKFKTKTNSGPSGMDAILCAINHFGQDS
VYKLPVGYNGYCRRNNGSPIKGWSAGFNMGKCEVKFANPNSSNKQSIGTFAGWEVESVRM
LDEDDYE

Enzyme Prediction     

No EC number prediction in ASPNIDRAFT2_1086727-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	133	469	1.1e-65	0.9493243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	6.53e-80	157	465	23	342	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.
214753	Glyco_18	5.01e-78	133	464	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	7.21e-73	133	462	1	343	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	1.13e-69	133	464	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.82e-59	135	464	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA66616.1|CBM18|GH18	0.0	8	1742	17	1753
BCS25298.1|CBM18|GH18	0.0	1	1743	10	1770
ANH56432.1|GH18	0.0	111	1745	37	1634
ALI93565.1|GH18	0.0	111	1745	37	1634
AIT18875.1|GH18	0.0	110	1747	62	1829

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUP_A	3.33e-48	152	465	114	439	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
5WV8_A	3.71e-47	152	465	114	439	Crystal structure of a mutant insect group III chitinase (CAD1-E217L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVB_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)6 (CAD1-E217L-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
3WL1_A	4.38e-47	133	473	8	366	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]
3WKZ_A	1.09e-46	133	473	8	366	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3WL0_A	2.72e-46	133	473	8	366	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36362|CHIT_MANSE	1.48e-44	133	473	24	382	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|P30922|CH3L1_BOVIN	1.14e-42	135	465	25	358	Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3
sp|Q9WTV1|CH3L1_RAT	2.70e-42	135	465	23	356	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
sp|Q91XA9|CHIA_MOUSE	3.21e-42	146	465	37	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	3.21e-42	146	465	37	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999774	CS pos: 23-24. Pr: 0.9775

TMHMM  Annotations     

There is no transmembrane helices in ASPNIDRAFT2_1086727-t41_1-p1.