CAZyme Information: ASPWEDRAFT_108842-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_108842-t33_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1607		176501.78	4.4761

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878211:217900-223158(+)

Full Sequence      

MAYSSQSRHSRSWEWRLLVLFILFNIFSTATAQFYVCNSTSPCVNGACCGVKPGEASGLC
GYDPDDQCSKANCVSNCDAKAECGKWAATAGAKCPLNVCCSSYGFCGTTSEFCDKGDDDN
KSCQSNCGSPTEPSCSSNDVLKKVIGYYESWASNSRRCDGWTPNQLPAQSLTHLSFAKNL
VRMLQKYGLNGADLDWEYPGADDRGGNSDDTENFAKLLRTIRDEFNASGQNYELSFTIPS
SYWYLRHFDVPKYLASGADWCNMMSYDLHGVWDGHDPYIGKVVGAHTNLTEIAQAMDLLW
RNDVDPSKIVLGIGFYGRSFTLSDPSCTKPGCPFSGGGANGTCTQTSGILSYKEIQEIIT
DSENVPVWEEEAGVMYLTWDENQWVSFDTNQTFKQKVDYANDHCLGGVMIWSNDQDTYDW
QALSALLGKTVDGGSLLQGSNSNDEDAKSLVHSYNKYTGGDCYISDCVDWNRGSCKKGYS
ILDYVHKGSLGVISDPDDKLCKTGDTTEDEDEDSQYRLICCPTDAMPTCSWTGGSPDGFC
TGGKDDTCGGNKFELVRDHYNDRTGSSPCTVNSRSLCCSTLNQLDQCSWTDCNEECEKSW
YRFSNFSLNAGPNLNQNNEYCTGTAEFCCPSKDTLKNCVWANCGESCPEKKLLVTRRNQL
WNPDVPHGQVGEYWCGDDEMMSMCCDPPSAGGEAPVDPADLFEYPDEDNVSWYEKTEPGA
NTEASDIEDEDPFGFVMIDGDTDAYDQSLVDQWTFLDDSGGALHSKRSTTEHNLFGSRDD
TFDHVEETYQIKCSSLLKNDTGCHSIFSGGASNTIVKMPANVGAAGPYARVISLTPRGST
TKRGNVLPRSAGQVYDMKVDYDLAAAGEEEKGDVNFRVDFTNLQGYWDKITDSPAKHKKR
WFGDFDAWLEKVTSIVKSEKGYLPLAYDGSVKLLELTQNCSGDSPYKLDLDTRLKVGLHA
QYAYYFEGAILPAPKMIASYAYFSINPSAELIFQLSGEATFQSTTGEADLIDGIPFSGLS
IKGLINIGPELGVTGSIDTSLTFAGELQAGVGVEFQKTEVYFPQDSDAKDATVKPSGLRD
NDREKEPAFLVTPMFESSATASGHINMNLTPKVRFGISVLGGKLSGGFVTAGVENTISVG
FDSSTTTSTSSGSSSDSFCYWADYLYSLFVQAEVKFPGDLIYWGSEKLELDSPDDAITLI
DKKCMPYEKNVKITPRDDINYSGSSDPPIAWDTSDQGNIIAVNPRTDGEPIFSALMACPG
TNDSVTDDGGDLCTIGSTKRATTNCDPPPALFYNCDYFPDLAVANNNKKTNGNKKTQTLT
GICNNIKGYLDSHKNAPGVGSNWMLLTYWKDPSESNRVQSCGQPGGPEKQCTDLKKSLWP
EDVQAQVKKDKNQFAARKMTGWKNDMSCDEFPFNACHQGGAGAATACAPAEQQDYQRDIN
GFIPNILDRDHGNRRGGDEPHYGKLANDVRQYSVNLFYGSQNDEKIGGYMNKGGVIYDDP
NGKNPSVNPGTKLNYVIGGVNLQSDRWRIKKNGKGLNALCVQSLPPVKVQNDDKMIMTYP
VQKCRVDFVAAKDVKKRGLDPYNTQHWVVDGEFTCFFFLSGKMLIYF

Enzyme Prediction     

No EC number prediction in ASPWEDRAFT_108842-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	175	420	3.4e-54	0.6858108108108109

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	7.58e-63	143	416	1	334	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	8.58e-62	176	416	100	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.
395573	Glyco_hydro_18	1.04e-55	175	416	91	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	1.81e-54	176	414	95	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.
119365	GH18_chitinase	1.10e-47	176	416	113	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	15	1590	45	1630
EGX48302.1|CBM18|GH18	6.50e-291	18	1573	12	1653
EGX53198.1|CBM18|GH18	1.39e-216	17	1436	8	1570
CAE7022350.1|CBM18|GH18	1.24e-205	19	1449	12	1574
EAA66640.1|GH18	3.03e-182	103	1440	4	1456

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	3.79e-37	175	418	104	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	4.23e-36	175	418	104	352	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
5WUS_A	9.59e-34	160	418	78	344	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]
1HKK_A	1.77e-33	175	418	97	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	1.81e-33	175	418	97	344	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	2.80e-33	81	419	317	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	5.82e-32	175	418	118	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P36362|CHIT_MANSE	1.10e-28	151	423	105	380	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	7.40e-27	160	418	98	363	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q91XA9|CHIA_MOUSE	2.67e-26	160	418	98	367	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000280	0.999692	CS pos: 32-33. Pr: 0.9717

TMHMM  Annotations     

Start	End
13	35