CAZyme Information: GAQ05331.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ05331.1
• CAZy Family: PL3
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A0S7DL08]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1293	BCLY01000004|CGC19	140572.36	5.4388

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000004:4215347-4220234(+)

Full Sequence      

MKQSLFFFTTLVAGAFSAHSGSHIHLHVSHRARTSEAIDARDDQGLDEWLAANKRAPPSA
LKACPLSCHETDNSSLGAGWFLFPDASRLAACNETMLFNFVVQTEVDGASSHGPKMGIRA
CTADYSSATQAAYEPHDERAALCPTPNHALVEASIRMSHSTAGNDDGFAVQDVLSAGHEI
VNYFRSQKPSCVENALAFGYSQSAVVGVFAGAEVHQHGVTTNVLNKLLDYVENNSVSETT
IVQLCQADGRGADYGISIIASSAKHLLVVQDAVKSWVKGRCVSAADGDEDWTTVTLRVPT
RVKSNSDAIGNMTLPTAAAHLGSRSRIAARAECQTTSVNPGDGCWALADRCKITDAKLKE
YNARPNFCNTLVAGEKVCCSSGTLPDTVPPGNPDGTCKTRQVVGGDICGSLASKCGLSLQ
EFYKVNTEANLCVNLKAGQHAQAQSRRILLHVHDQAGDDCYGIAAANGITITDLEDFNKN
TWGWSGCKILPLNFKLCVSSGSPPMPAPVPNAICGLTVPGTKEPAKGAELSTLNPCPLKV
CCNVWGQCGTTDDFCTVSKSETGAPGTSAPGKNGCVSNCGRDIVNSGPPDRTIHVAYFEA
WNHKRKCLTMDVGQIDMDKYTHIHFAFADVTKDFNVDISAVKEQFDLFKGMSGVKKIISF
GGWDFSTMPGTFNILREAVKPANRDIFQKNLVAFAPDIPDIPPGDPEAGRDYYYLLSNVK
KAFGVGLRQQVDFVRLSQRQLFEVHINDTETRDALSMITKAGVPSRKVVVGVTSYGRSFK
MAEAGCTGPMCKFTGTSRISNAAKGRCTDAGGYISNAEIAEIISSGKVTKQWTDVGSNFL
VYNDTEWVAYMYDDMKAARAKFYDSYNFAGTTDWAVDLQAFRDGSGGDDYPDDYEPYIDT
SMYPECQYIFNVEVAVMEAALEKYKDLVNNGYDEKFKIYEGYVDEQVQDQIDAFMGSGKA
DKYFKCTETKDVMCCSKCNIPQCMVDCDKSKDCNGRATVDIKCPTTLKSGSSTIIAVGHH
FPNATYTLQDPEGFWKDIGAEYGIEESWVKFGRRHIRAGNGCQYAGEDVNDCIDKQISGF
YNYPMKDTVKVYTPKDIIGDSYDKTEDLLNRLKIVRDNVDYDDLMQWSDLVDAGSLPALT
IRTAVESLLFFIPFVGEAAGATGLTAVRSMLRMAGAAGETGLLVHDIIEHPENAFISVFS
YLAGAGVGRTGFKNAANARRSMKASDIDILGSMKVDLDLIQTWEYLEEAVAKDQIQALPT
RIMVGSSNTQEAWDLLRQGKTRGERLIIHPTSD

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	6.97e-137	595	879	3	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	6.22e-32	595	878	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	1.41e-22	595	877	3	305	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	9.03e-17	595	891	2	353	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.
225862	ChiA	3.67e-10	589	890	35	441	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI73538.1|CBM18|CBM50|GH18	0.0	36	1241	40	1359
QYT01306.1|CBM18|CBM50|GH18	0.0	39	1237	28	1354
CAP66963.1|CBM18|CBM50|GH18	0.0	28	1240	21	1353
CDP28705.1|CBM18|CBM50|GH18	0.0	28	1240	21	1353
VBB80335.1|CBM18|CBM50|GH18	0.0	28	1240	21	1353

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL0_A	1.34e-08	595	882	10	362	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
3W4R_A	1.94e-08	584	882	16	380	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
4P8U_A	2.12e-08	762	881	237	348	The crystal structures of YKL-39 in the absence of chitooligosaccharides was solved to resolutions of 2.4 angstrom [Homo sapiens],4P8V_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc2) were solved to resolutions of 1.5 angstrom [Homo sapiens],4P8W_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc4) were solved to resolutions of 1.9 angstrom [Homo sapiens],4P8X_A The crystal structures of YKL-39 in the presence of chitooligosaccharides (GlcNAc6) were solved to resolutions of 2.48 angstrom [Homo sapiens]
3WKZ_A	2.34e-08	595	882	10	362	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3WL1_A	2.34e-08	595	882	10	362	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	6.01e-65	193	903	73	738	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|Q28990|OVGP1_PIG	9.57e-08	595	882	25	363	Oviduct-specific glycoprotein OS=Sus scrofa OX=9823 GN=OVGP1 PE=2 SV=1
sp|Q28542|OVGP1_SHEEP	9.75e-08	595	882	25	363	Oviduct-specific glycoprotein OS=Ovis aries OX=9940 GN=OVGP1 PE=1 SV=1
sp|P36718|OVGP1_PAPAN	2.46e-07	595	882	25	363	Oviduct-specific glycoprotein OS=Papio anubis OX=9555 GN=OVGP1 PE=2 SV=2
sp|Q12889|OVGP1_HUMAN	2.58e-07	595	882	25	363	Oviduct-specific glycoprotein OS=Homo sapiens OX=9606 GN=OVGP1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.207627	0.792351	CS pos: 20-21. Pr: 0.7042

TMHMM  Annotations     

There is no transmembrane helices in GAQ05331.1.