CAZyme Information: An19g00100-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An19g00100-T-p1
• CAZy Family: GT62
• CAZyme Description: Putative chitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1113	An19_A_niger_CBS_513_88|CGC1	123805.63	4.7295

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

• Gene Location: location=An19_A_niger_CBS_513_88:25786-29548(+)

Full Sequence      

MALRTGTGLLALSFAFLAIFCNISTVLAQSCSASNPCATGCCSKYGYCGTGEDHCGADCI
ANCDYEATTECSATKPCAEGCCSKFGVCGYGPDYCGKENCVANCERTSECDPGNWGLEYS
SSSTCPLNVCCSKYGFCGTTEEFCGDKKVKRPSCVPSQRLRRVVGYYEGWATTRPCKAFW
PEQIPKGVYTHLNYAFATIDPITFEVLPPTALEAKLMTRLTSLKDHDPGLRVNIAIGGWS
FNDPGTTASVFTQLAASEDNQMKFFRSLASFMATYNFDGVDIDWEYPVDSDRSGRKEDFQ
NFPKFMLNLKNALKGTGGRDELSLTLPTSYWYLRNFDIKALAKSVDYFNYMSYDLHGTWD
KGNKWTGEYLDAHTNLTEITDSLDLLWRNDISPDKVVMGVAFYSRAFTVEDTKCMDPGCR
FVSVSDPGDCSRQTGILMNSELDDIRANKSLTPSLDKEAAVQILKWGNQWASYDDKTTFK
LRIDFAKKTCLGGIMVWAVSHDTYDGAYSSALASISPQIKPIKKLQVSPNGLTVTRDERI
RQCKWTSCGQTCPSDYVAISRSDPKYRKGELMLDSIRCPKGASHTLCCPKEDVPKCGWYT
HNNGNCSPDCPSGYFEIGSISSNGLCHHDYEAACCESNKDSTGLYNTLQWSEAPMCDWGE
CPVVDDKKSTTLALATAGSGDADKKTWDNCDWYDSVDSPPKGKPDDYCVDSCPSDMVRLA
TYRYDENCAGGVRAFCCTDNYYTSKSQTNPEMADFRSSLNNYLEDGTCSMGESASLSRRD
VFGRDTDKYEDLQFLIPLLYTLLVKNDTDLNAKEKLEAGYWDDWAKSNSLTGLVLSTLRS
FVRQTRLWYEMGGKYVAQNILCRPTTWNDMAQQKSIPVCQGDPCDEGADPDLCRTAELDG
ETDYDDDDDDGSSSSDEDDGTLDKRMLSAPSHGTLEKRAAPKTYKVWCAGTGDWVDGLKI
KPVYYPSAGRWQPTDVQYKEARTYQSRTDCANPLVDPMEKDANNYDTEHVLELQMVPMFF
RFATTGELTSGRTASFQPIDCTFFLPTSQGGIDFLHQSVMPKAEIYPGDPYEDRRAKSPE
FRIMAALGTSKNKENFYLLEKAVNGMKARVSTR

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	161	505	1.8e-64	0.9459459459459459

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.22e-76	162	502	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	2.32e-74	164	499	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	1.80e-67	163	506	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	4.02e-66	162	502	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.81e-52	163	502	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	1113	1	1113
EAA66648.1|CBM18|GH18	5.48e-255	11	1110	8	1107
APA10647.1|CBM18|GH18	2.07e-241	28	1107	18	1061
CEI63500.1|CBM18|GH18	3.10e-241	19	1108	12	1038
QPC58010.1|CBM18|GH18	7.45e-236	28	868	21	830

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HKK_A	1.34e-39	162	506	2	346	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.37e-39	162	506	2	346	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	1.37e-39	162	506	2	346	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	1.40e-39	162	506	2	346	Structure of human chitotriosidase [Homo sapiens]
3WL1_A	1.44e-39	162	506	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.47e-39	170	505	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	2.96e-38	155	506	16	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q91Z98|CHIL4_MOUSE	4.34e-37	166	508	27	371	Chitinase-like protein 4 OS=Mus musculus OX=10090 GN=Chil4 PE=1 SV=2
sp|P36362|CHIT_MANSE	1.24e-36	153	506	15	379	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|O35744|CHIL3_MOUSE	6.04e-36	166	508	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	0.999734	CS pos: 28-29. Pr: 0.9769

TMHMM  Annotations     

Start	End
7	29