CAZyme Information: ASPTUDRAFT_59063-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_59063-t33_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1542		168034.03	4.0966

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878207:782447-788554(-)

Full Sequence      

MPRISAARRGPPWNSLFVALIVLCLSVQVQTQTTYHCNATTPCYNGACCGVTDGQGICGY
GSDFCGDTCVSNCNATAPCGQYAAVPGTTCPLNVCCSRYGFCGTESDFCNADCQSNCAAP
IEPGCTTNDVLRRVIGYYEGWSSDRVCDSWSPSNIAASALTHLHSWALSVLNMLETYGFD
GVDLDWEYPVSSDRGGKAADKENYVALISELRNALDNSGKTYGISFTTPSSYWYLQNFDV
PGMLKAGADWTNIMTYDLHGTWDASDVWIGSVMLAHTNMTEIKSALDLMWRSGVDASDIV
LGIGFYGRSYTMSDTACYQPGCPFIGAGNAGSCTATPGVLSFSEIMELMQDEDTEVFWDE
TDAVNYMVWDDQWVSFDTNVTFQQKVEYANTKCLGGLMIWSVDQDTYDWQALSGLLGKSV
ASNNLLSGGTLGNSDKKDLSRIYSAFTGTDCYVSECFYWNSGWCETGYSTLDYVHQGLYG
IIADPDTMTCATGEEGDTDAQYRMICCPTDAMPESCAWAGSTVSDQCGGPGCTSGQYELV
ADSYVDRTGSEKCARSSRPLCCNTDSALEKCSWGMCGQGSFCCPSEDTYTGCDWYGCDEK
CPNTKVLITQRSEIIQDGNAVTCTSGANKLCCDPPDGSNSWPVDPEDLFKYPDEENVSYY
YSVQESSNDEDTDNASEDPFALVMIDGDASAYDESLVDQWTFLDDESELSKRGLKMHKRH
NLFEQRNDTFDNVIETYHIQCVSLFVNGSACTSIFNGGASNTIVKMPADIGAGPYARVIN
LFPVGSDISDMKARSTGEVYELTVDYDFAAAAEEQKGDVNFRIDYTNLQEYWEDITDTPA
SRKRWFGSFDNWLKKMTTIVKDEKGSLPLDYEETIKLFHGHEYCPAWNTDATFDIDAFIH
LELSGQYGYYFEGSILPTPNLISAYGYFSIEPSAAILLTIRANAIMQSATGSAELFSLGF
PGMSIKGLINIGPELALYGQLDASLQVSGELNAGVALLFKRTEVYFPQDAAGAAASVAPA
DLDDDDDATYSFDPTFDAQLNAEGNLALSLTPEVRFGVSVLGGDLMSGYVTAGISNTINL
GISAEASYSGDEASAGFCYWADYVYSIFLRADMSFLGDVAYWGGNYDVTSPSDPLELVSK
TCTSYSSGDALTKRTDTESLVANTTGSACFGGIISCQTIEDNTKTASNLTCPIACDGADS
SSCTILDTAPDPESSSRKRQGPASGATNGICYHWPALWYNCAWFPDKNLQNLDSNTNTLP
NNKYWTAPVLSLFAGICRNVASYLYQHQASWSPGYMGPDFMRLTYKKSGKKSPNRAAACG
SSTSGNTPAGECSRIKRSLWPAAVQKAVAAKDPNYKSMQGWSDPVSCDEFPCGAAEGGAG
AATACAPVEQQAYQALANNMIPQIRDNSVNMFWSATSFTGYPQHFTVNLFNTYSTQHITN
SLGPYGGYYDSGENLPLTEIAAGVNLFSSPIWTLSNNNAVCRMDGGPPREDMDKRIWYYR
LAPCQVVYEDPNQSGRWYKRDDDDSYDGPDHLHPRYWQIKGA

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	144	408	2.4e-51	0.722972972972973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	3.54e-61	169	405	103	341	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	3.68e-59	133	405	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	6.65e-55	135	403	3	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	8.33e-51	169	405	95	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	2.49e-45	169	405	116	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
QGA22188.1|CBM18|GH18	0.0	4	1481	36	1584
EGX48302.1|CBM18|GH18	5.89e-281	10	1481	3	1617
EGX53198.1|CBM18|GH18	5.50e-199	32	1117	26	1272
CAE7022350.1|CBM18|GH18	2.64e-188	17	1401	11	1569
EAA66640.1|GH18	9.63e-174	120	1484	31	1576

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	5.43e-36	140	407	84	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5WUS_A	3.46e-35	151	428	84	365	Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
6JM8_A	6.04e-35	140	407	84	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
5WVF_A	3.73e-34	151	428	84	365	Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
5Y2A_A	5.50e-34	140	407	82	350	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis],5Y2A_B Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 2 [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13231|CHIT1_HUMAN	7.41e-32	169	407	122	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P09805|KTXA_KLULA	4.10e-30	138	384	446	676	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-27	169	407	122	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|P36362|CHIT_MANSE	7.76e-27	140	414	104	382	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	9.41e-27	169	407	122	363	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000288	0.999691	CS pos: 31-32. Pr: 0.9732

TMHMM  Annotations     

There is no transmembrane helices in ASPTUDRAFT_59063-t33_1-p1.