dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: EAW17011.1

You are here: Home > Sequence: EAW17011.1

Basic Information help

Species

Aspergillus fischeri

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri

CAZyme ID

EAW17011.1

CAZy Family

CE16

CAZyme Description

chitinase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355		40013.15	4.9072

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in EAW17011.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	18	341	5.2e-65	0.8614864864864865

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	6.62e-84	28	342	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.
214753	Glyco_18	6.67e-83	23	342	22	333	Glyco_18 domain.
119357	GH18_zymocin_alpha	3.90e-81	23	343	24	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.
395573	Glyco_hydro_18	7.61e-69	23	341	19	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.95e-61	26	341	25	320	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.71e-174	16	342	50	376
2.37e-170	47	342	1	296
1.39e-166	27	342	183	498
1.39e-166	27	342	183	498
3.11e-162	27	343	102	418

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.52e-50	28	339	34	346	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
9.69e-49	28	339	34	346	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1.21e-45	28	342	123	437	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]
1.71e-44	28	342	123	437	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]
4.37e-44	28	342	32	341	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.96e-45	28	342	52	364	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
3.81e-45	28	342	52	364	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
7.54e-42	28	342	52	364	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
2.50e-41	26	349	51	383	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
4.93e-41	28	342	52	362	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000004

TMHMM Annotations help

There is no transmembrane helices in EAW17011.1.