dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: KAB8208432.1

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Basic Information help

Species

Aspergillus parasiticus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus

CAZyme ID

KAB8208432.1

CAZy Family

GH5

CAZyme Description

glycosyl hydrolases family 18-domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
449	ML734951\|CGC2	49351.25	6.9563

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AparasiticusCBS117618	14005	N/A	253	13752

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.14:12	3.2.1.-:6

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	103	442	3.8e-79	0.956081081081081

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.46e-106	104	436	1	334	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	2.22e-104	132	437	29	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	2.00e-92	104	436	1	307	Glycosyl hydrolases family 18.
119365	GH18_chitinase	9.74e-87	105	436	1	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.
119357	GH18_zymocin_alpha	1.38e-78	107	436	4	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.59e-303	24	449	11	436
1.54e-276	68	449	6	387
4.41e-276	68	449	6	387
1.64e-271	68	449	6	387
4.07e-268	79	449	1	371

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.32e-61	103	437	4	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
1.99e-60	103	437	4	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
2.23e-59	99	439	4	362	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]
3.86e-59	109	437	10	343	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
3.97e-59	109	437	10	343	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.52e-58	97	437	17	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
7.69e-57	99	439	20	378	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
4.12e-56	108	437	27	366	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
8.05e-56	108	437	27	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
4.19e-55	108	437	27	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000193	0.999770	CS pos: 28-29. Pr: 0.9273

TMHMM Annotations help

There is no transmembrane helices in KAB8208432.1.