CAZyme Information: PWY82995.1

Basic Information

• Species: Aspergillus heteromorphus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
• CAZyme ID: PWY82995.1
• CAZy Family: GH32
• CAZyme Description: glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
537		59349.51	4.6316

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55	11436	1448321	306	11130

• Gene Location: location=MSFL01000011:551832-553689(-)

Full Sequence      

MATPSVFSYLLFLLLGWQLVFSAALSDNVTNAAFPSDFNNLLVAQEYTCTKSQRCERGCC
GPIDDTGTGNCGFGPDFCGDKCNSDCDRKAECDPGWGTQWSQMSTCPLNVCCSKFGFCGT
SHDFCGDKVVVSPQCNGNSASNRTIGYYEAWNLERPCGKMGPKDIPLGYYTHINFAFAYI
DPQTFRIAPMDNTTAPLYRPVTALKGRQSGLKVWIAVGGWAMNDPGPSKTTFSDLAASEA
SQDTFFDSLLSFMQSNNFDGVDLDWEYPVADDRGGRPEDFANYVTLLKRLRERLNQSGNH
YGVSITLPASYWYLRGFDIVNLEPHVDFFNIMTYDIHGVWDSTNKEIGSFAHAHTNLTEI
NAGLELLWRNNINPERVNLGLGFYARSFTMKDPSCMKPGCPFTGGARAGECSGTEGVLAE
YEINKIIQKGGAEVTLYKDEAVKVVTWDKDQWASWDDQETMKLKIQYANQRCLGGTMVWA
IDLDDGTLVGELGKAQGKNRSHTLPENPQLFPDLGTVDVDDLLGWKKATDNRTGGGE

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	142	486	1.1e-70	0.9425675675675675

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.21e-88	143	484	1	334	Glyco_18 domain.
119357	GH18_zymocin_alpha	2.38e-84	143	484	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.
119351	GH18_chitolectin_chitotriosidase	1.66e-82	147	485	4	342	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	5.41e-76	143	484	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.66e-66	145	484	2	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
CAK42254.1|CBM18|GH18	3.20e-290	5	527	2	534
BCS02338.1|CBM18|GH18	6.61e-286	5	527	2	534
BCS14016.1|CBM18|GH18	6.61e-286	5	527	2	534
QBJ27663.1|CBM18|GH18	6.50e-274	5	487	2	494
QRD82868.1|CBM18|GH18	1.02e-241	46	515	39	509

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUP_A	9.76e-48	143	485	94	439	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
5WV8_A	1.31e-46	143	485	94	439	Crystal structure of a mutant insect group III chitinase (CAD1-E217L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVB_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)6 (CAD1-E217L-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
5WUS_A	4.24e-45	143	485	3	343	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]
6JM7_A	2.02e-44	145	485	7	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5WVF_A	5.63e-44	143	485	3	343	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q91XA9|CHIA_MOUSE	7.32e-44	145	508	25	400	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	6.63e-42	145	519	25	404	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q13231|CHIT1_HUMAN	8.09e-42	143	514	23	397	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9BZP6|CHIA_HUMAN	8.47e-40	147	508	27	400	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	9.48e-40	129	485	1897	2254	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000275	0.999693	CS pos: 22-23. Pr: 0.9763

TMHMM  Annotations     

Start	End
7	26