CAZyme Information: P168DRAFT_321807-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_321807-t37_1-p1
• CAZy Family: GT90
• CAZyme Description: glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
783		84790.98	5.2882

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcampestrisIBT28561	9929	1392248	173	9756

• Gene Location: location=MSFM01000013:220555-223218(-)

Full Sequence      

MTPAWLSTAAWALGLLLYVEGGSAIGTPDLRKPASPGYRGSDPCPTSCRITGPNPSNWSA
YHNFEQLQSCKQSLFYEFSLYDKVDDPETLHRIYACASNGEDWYNLPQSQKKVKTTVESV
DSTYQIGWWADGALSATGISAVLEQMRRYLKVDHAASKNSTFLFARLGSASVGVYIGKGL
QKESVSSFALRTAEHNIAKLPVNTGTVAMQLCDQNKDSGFTFGLIASSNGTFASVQDAMK
TWAKGGCLSFHDSKNITGTAALTTPLFSSTKATKSKLVSSSISSLGAKQSATLPDLAPKP
GADGSCATYTVQPDDNCSNLAAAYSLTIAELEEFNKNTWGWNGCSNVWKGTVMCLSTGTP
PMPAPLENAVCGPQMPGTPIPSDTTNLTHLNPCPLNACCNVWGQCGITDEFCIDTSTGAP
GSSEQGTAGCISNCGTQLVRSDAPEVFRSIAYYQGYSFNGRQCLYQDALQIDGSKYTHLH
FAFATLTDDYEVVFEDKIMEYEFSNFLKIAGPKKILSFGGWGFSTNPDTYHIFRQGVKPA
NRLKFATNVANFIEDRGVDGVDIDWEYPGAPDMPGIPLPTKTTARTISPFSLSSKICSGG
SRFQSQRRLRMCLRSHVNLTETMSSMVMITKAGVPSNKVVIGMTSYARSFAMADPECYGP
ECFFTGAPTDSPATKGVCTATGGYIADAEINEIISNSSRVNQQYTDSTSHSSILVYDNDQ
WAAYMSPAIKAARKTLYKNLNMGGSSDWATDLQEYNDPPNNGTTWADFKEMVNNGEDPWE
VEN

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	1.09e-135	448	753	1	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	3.38e-33	448	752	1	333	Glyco_18 domain.
395573	Glyco_hydro_18	7.47e-27	448	751	1	305	Glycosyl hydrolases family 18.
119349	GH18_chitinase-like	1.33e-21	450	577	2	124	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	4.63e-20	477	752	29	340	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
AEO62937.1|CBM18|CBM50|GH18	3.26e-262	31	778	24	874
AIT18887.1|CBM18|GH18	2.25e-257	5	780	5	873
QQK44152.1|CBM18|CBM50|GH18	1.78e-256	15	783	28	904
BCS04716.1|CBM18|GH18	1.55e-255	5	778	6	873
BCS16285.1|CBM18|GH18	1.55e-255	5	778	6	873

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Y29_A	9.65e-14	447	755	7	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
6JAV_A	1.05e-13	447	755	7	353	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]
1SYT_A	4.81e-13	447	755	1	337	Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
1LJY_A	4.81e-13	447	755	1	337	Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution [Capra hircus]
1HKK_A	4.93e-13	471	755	25	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.59e-66	294	783	241	736	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	4.72e-13	471	755	46	367	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q15782|CH3L2_HUMAN	4.04e-12	438	755	18	367	Chitinase-3-like protein 2 OS=Homo sapiens OX=9606 GN=CHI3L2 PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	4.38e-12	471	755	46	365	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	5.94e-12	477	755	52	367	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000251	0.999721	CS pos: 24-25. Pr: 0.8810

TMHMM  Annotations     

There is no transmembrane helices in P168DRAFT_321807-t37_1-p1.