dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus aculeatus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus aculeatus

CAZyme ID

ASPACDRAFT_51022-t33_1-p1

CAZy Family

GH51

CAZyme Description

glycoside hydrolase family 18 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761	KV878973\|CGC4	80044.06	4.0231

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AaculeatusATCC16872	11165	690307	322	10843

Gene Location

Enzyme Prediction help

EC	3.2.1.14:2

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	232	361	1e-16	0.3547297297297297

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.25e-41	126	360	3	332	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	3.90e-40	142	360	19	339	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	6.37e-34	126	360	3	305	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	2.23e-26	126	338	3	321	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.
119349	GH18_chitinase-like	3.19e-23	125	251	1	144	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.56e-177	1	552	1	683
2.15e-124	15	478	21	589
1.71e-115	153	553	24	566
1.06e-77	172	478	2	411
1.96e-71	10	492	5	581

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.08e-21	126	360	4	340	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1.10e-21	126	360	4	340	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1.10e-21	126	360	4	340	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]
1.11e-21	126	360	4	340	Structure of human chitotriosidase [Homo sapiens]
1.28e-21	126	360	4	340	Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.24e-21	121	360	20	361	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
4.67e-19	126	360	33	364	Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3
3.40e-18	126	360	25	355	Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2
3.81e-18	121	360	20	359	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
4.44e-18	126	360	52	382	Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000270	0.999723	CS pos: 25-26. Pr: 0.9374

TMHMM Annotations help

There is no transmembrane helices in ASPACDRAFT_51022-t33_1-p1.

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