CAZyme Information: ASPSYDRAFT_29731-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_29731-t33_1-p1
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442		48476.37	4.7050

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878584:2456532-2457981(+)

Full Sequence      

MMLKPVALALAALQCVAGLRFAMYIDQYHTDGLPGSNTTQGITHAIMGFAKSTDFNTDSG
SSFKPFEPVETMRKRFVPDTKVLVAIGGWGDTEGFSTGAKDEASRERYAKNVAKMLDDNG
FDGVDVDWEYPGGNGEDYKKVPNKDKVGEIETFPLFIQALRKAIGKEKLLTIATPGKRED
MIAYTEENGPKIWPSVDFVNVMAYDLMNRRNNVTKHHSSVVDSHDTIKAYLEIGAPPEKL
NLGIAYYMKWFTTQENADCDTHPIGCPTVEMEAANGDDNGKSGTITFETKNMAPPPQDLK
VSTDQKCGLEAKTKCPAGSCCSIYGSCGSGDDYCGANCDSNYGECKGTSIQGSLQSALKD
GKTDEEAGGQYYMDVKSNLFWTWDTPELITRKFKEIVDAEKLGGVMAWSLGEDTYKWEHL
KAMQAGVAERGGNTEARDDPER

Enzyme Prediction     

EC	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	35	421	1.5e-57	0.8783783783783784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	2.10e-82	20	413	1	307	Glycosyl hydrolases family 18.
214753	Glyco_18	2.19e-52	21	413	9	334	Glyco_18 domain.
119365	GH18_chitinase	4.08e-47	22	247	9	262	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.
119349	GH18_chitinase-like	1.48e-45	21	206	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	8.44e-39	43	269	29	262	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
BCS22836.1|CBM18|GH18	1.11e-315	1	441	1	441
EAA60035.1|CBM18|GH18	7.45e-229	26	434	473	881
BAE63426.1|CBM18|GH18	2.46e-217	4	430	4	430
UDD62778.1|CBM18|GH18	2.46e-217	4	430	4	430
QRD94346.1|CBM18|GH18	9.98e-217	4	430	4	430

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	1.14e-24	32	247	44	261	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	1.46e-24	32	247	63	280	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6KXN_A	7.78e-22	74	292	70	289	Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KST_A	7.78e-22	74	292	70	289	Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KST_B Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KXL_A Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXL_B Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
1D2K_A	2.40e-21	81	293	88	304	Chain A, CHITINASE 1 [Coccidioides immitis],1LL4_A Chain A, Chitinase 1 [Coccidioides immitis],1LL4_B Chain B, Chitinase 1 [Coccidioides immitis],1LL4_C Chain C, Chitinase 1 [Coccidioides immitis],1LL4_D Chain D, Chitinase 1 [Coccidioides immitis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9D7Q1|CHIT1_MOUSE	6.61e-21	26	269	32	286	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|C5P230|CHI1_COCP7	1.68e-20	81	293	123	339	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
sp|P0CB51|CHI1_COCPS	1.68e-20	81	293	123	339	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
sp|Q1E3R8|CHI1_COCIM	1.68e-20	81	293	123	339	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
sp|Q13231|CHIT1_HUMAN	5.93e-18	43	269	52	286	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000257	0.999700	CS pos: 18-19. Pr: 0.9704

TMHMM  Annotations     

There is no transmembrane helices in ASPSYDRAFT_29731-t33_1-p1.