CAZyme Information: P175DRAFT_0524620-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0524620-t39_1-p1
• CAZy Family: GT20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
480		54389.63	6.6594

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000005:2208534-2209976(+)

Full Sequence      

MGTFEKCIFLGCILALAGITLFSHPDHHESKVIQEPWGIPCDDRHPCQSGCCSHSGICGV
GPEYCGADTCIDCRTRARPRSKTSHLRRFVGYYELWSADRPCNRMAAFELPSATYAHVNL
AFITIDPTTFEVVPIPAAHANAIQRFTQRKKYDPDLRVFVTVSGLAPHDWSKPDASVFSR
LARSDAHQTVFLRSLTSFISTYDIDGVDINWEHPDGFSDDYENLPKLMQNIRSALLLTGG
RYGLSMTLPVSLPNLHHYNLRRLPRYVDYFNLMPLDLHSQLQMGDTWQGQSLGPVVNMTQ
VEEAMDLLWRNHVMPDNVNFGIALYSASLVPADRECTHVGCPALSGATPGFSSLKQGMLM
NSEVQDLMDPAFHERAHGRLYHRHDWGSRALQYSVLDADAGVRISQNKHQWIAYEDRETL
EKKLESARDLGFGGVVVWAMSHDTYNADYTKVLDCLLEEKFHRRKSLQYHYCNEIQLHQV

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	87	450	7.3e-45	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.38e-44	90	443	3	334	Glyco_18 domain.
395573	Glyco_hydro_18	7.16e-44	88	443	1	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	2.51e-34	90	439	3	341	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.
119349	GH18_chitinase-like	2.55e-33	89	277	1	178	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
119351	GH18_chitolectin_chitotriosidase	1.32e-31	90	439	2	337	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ82859.1|CBM18|GH18	3.60e-93	51	458	905	1296
QPC58010.1|CBM18|GH18	1.78e-88	41	461	24	475
CAK47333.1|CBM18|GH18	3.00e-88	41	453	31	512
BCS04193.1|GH18	4.82e-88	57	461	50	436
BCS15787.1|GH18	2.47e-86	63	461	68	448

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WL1_A	8.92e-20	88	445	8	361	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]
3W4R_A	2.09e-19	88	445	26	379	Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
3WKZ_A	2.17e-19	88	445	8	361	Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
3WL0_A	5.28e-19	88	445	8	361	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
5WUS_A	8.23e-19	92	445	7	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36362|CHIT_MANSE	8.06e-19	88	445	24	377	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q13231|CHIT1_HUMAN	1.06e-16	88	445	23	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P30922|CH3L1_BOVIN	6.62e-16	88	449	23	363	Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3
sp|Q8SPQ0|CH3L1_CAPHI	8.88e-16	88	449	23	363	Chitinase-3-like protein 1 OS=Capra hircus OX=9925 GN=CHI3L1 PE=1 SV=1
sp|Q7YS85|CH3L1_BUBBU	1.19e-15	88	449	23	363	Chitinase-3-like protein 1 OS=Bubalus bubalis OX=89462 GN=CHI3L1 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.019173	0.980788	CS pos: 25-26. Pr: 0.7479

TMHMM  Annotations     

There is no transmembrane helices in P175DRAFT_0524620-t39_1-p1.