CAZyme Information: ASPNIDRAFT2_1165650-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ASPNIDRAFT2_1165650-t41_1-p1
• CAZy Family: GH5
• CAZyme Description: Carbohydrate-Binding Module Family 18 / Glycoside Hydrolase Family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1291		144552.94	4.7005

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=ACJE01000011.1:52725-56973(+)

Full Sequence      

MALRTGTGLLALSFVFLAIFCNISTVLAQSCSASNPCATGCCSKYGYCGTGEDHCGADCI
ANCDYEATTECSAIKPCAEGCCSKFGVCGYGPDYCGKENCVANCERTSECDPGNWGLEYS
SSSTCPLNVCCSKYGFCGTTEEFCGDKKVKRPSCVPSQRLRRVVGYYEGWATTRPCKAFW
PEQIPKGVYTHLNYAFATIDPITFEVLPPTALEAKLMTRLTSLKDHDPGLRVNIAIGGWS
FNDPGTTASVFTRLAASEDNQMKFFRSLASFMATYNFDGVDIDWEYPVDSDRSGQKEDFQ
NFPKFISNLKNALKGTGGRDELSLTLPTSYWYLRNFDIKALAKSVDYFNYMSYDLHGTWD
KGNKWTGEYLDAHTNLTEITDSLDLLWRNDISPDKVVMGVAFYSRAFTVEDTKCMRNTDA
CCCAFRDPGCRFVSGSDPGECSRQTGILMNSELDDIRANKSLTPSLDKEAAVQILKWGNQ
WASYDDKTTFKLRIDFAKKTCLGGIMVWAVSHDTYDGAYSSALASISPQTKPIKKLQVSP
DGLTVTRDERIRQCKWTSCGQTCPSDYVAISRSDPKYRKGELMLDSIRCPKGASHTLCCP
KEDVPKCGWYTHNNGNCSPDCPSGYFEIGSISSNGLCHHDYEAACCESNKDSTGLYNTLQ
WSEAPMCDWGECPVVDDKKSTTLALATAGSGDAVCNVRSFSWDDGIAVQERKLCYDSTQD
KKTWDNCDWYDSVDSPPKGKPDDYCVDSCPSDMVRLATYRYDKNCAGGVRAFCCTDNYYS
SKSQTNPEMAGFRSSLNNYLEDGTCSMGESASLSRRDLFGRDTNKYEDLQFLIPLLYTLL
VKDDTDLNAKEKLEAGYWDDWAKSNSLTGLVLSTLRSFVRQTRLWYEMGGKYVAQNILCR
PTTWNDMAQQKSIPVCQGDPCDEGADPDLCRTAELDGETDYDDDDDDGSSSSDEDDGTLD
KRMLSAPSHGTLEKRAAPKTYKVWCAGTGDWVDGLKIKPVYYPSAGRWQPTDVQYKEART
YQSRTDCANPLVDPMEKDGNNYDTEHVLELQMVPMFFRFATTGELTSGRTASFQPIDCTF
FLPTSQGGIDFLHQSVMPKAEIYPGDPYEDRRAKSPEFRIMAALGTSKNKENFYLLEKAV
NGMKARIFRNVDLVDQTKWAGFIEDTSNPGIPLKEIKAAIAVWHYLNDQDVKNSFVELVS
HLREVWVEVDSRFNNNQPLFLPAWDEWWHDYIEYQVERTSTWITNGIAAMRKVWSDENHD
NDPAKLIVLAALTELEAFEVEIVRYNHLIFP

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	161	516	1.4e-64	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	9.45e-74	162	513	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	1.40e-72	164	510	3	342	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.
119351	GH18_chitolectin_chitotriosidase	1.79e-66	163	517	1	345	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.
395573	Glyco_hydro_18	1.60e-65	162	513	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	3.45e-50	163	513	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK47333.1|CBM18|GH18	0.0	1	1147	1	1110
APA10647.1|CBM18|GH18	6.99e-266	28	1254	18	1178
EAA66648.1|CBM18|GH18	1.01e-265	11	1209	8	1165
ATY64693.1|CBM18|GH18	6.22e-254	2	1282	3	1300
CEI63500.1|CBM18|GH18	3.31e-253	19	1227	12	1123

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL1_A	2.55e-41	162	517	8	363	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	6.32e-41	162	517	8	363	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3WL0_A	1.57e-40	162	517	8	363	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
3W4R_A	4.70e-40	162	517	26	381	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
1HKK_A	1.36e-38	162	517	2	346	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|P36362|CHIT_MANSE	6.17e-38	153	517	15	379	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|P09805|KTXA_KLULA	1.71e-37	170	516	389	715	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|Q13231|CHIT1_HUMAN	2.97e-37	155	517	16	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q91Z98|CHIL4_MOUSE	2.40e-36	166	519	27	371	Chitinase-like protein 4 OS=Mus musculus OX=10090 GN=Chil4 PE=1 SV=2
sp|O35744|CHIL3_MOUSE	2.02e-34	166	519	27	371	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000258	0.999718	CS pos: 28-29. Pr: 0.9763

TMHMM  Annotations     

Start	End
7	29