dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus niger

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger

CAZyme ID

An12g05330-T-p1

CAZy Family

GH7

CAZyme Description

Putative chitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
947	An12_A_niger_CBS_513_88\|CGC12	104078.93	4.2260

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

Gene Location

Enzyme Prediction help

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	299	512	1.6e-24	0.6216216216216216

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	6.75e-103	240	513	2	344	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.
214753	Glyco_18	3.86e-19	302	513	111	333	Glyco_18 domain.
395573	Glyco_hydro_18	7.83e-17	299	512	105	305	Glycosyl hydrolases family 18.
199914	M35_deuterolysin_like	2.34e-16	568	760	2	167	Peptidase M35 domain of deuterolysins and related proteins. This family M35 Zn2+-metallopeptidase extracellular domain is found in fungal deutrolysins (acid metalloproteinase, neutral proteinase II), including some well-characterized metallopeptidase domains in Aspergillus oryzae (NpII), Aspergillus fumigatus (MEP20), Penicillium roqueforti (protease II) and Emericella nidulans (PepJ peptidase). The neutral proteinase II from Aspergillus oryzae (NpII) unfolds reversibly upon incubation at higher temperatures, and loss in activity is mainly due to autoproteolysis. MEP20 is encoded by the mepB gene, which appears to be associated with the cytoplasmic degradation of small peptides. PepJ peptidase is a thermostable enzyme released under carbon starvation. Most members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands. The aspzincin motif is poorly conserved in one subgroup, that includes Asp f2, a major allergen from Aspergillus fumigatus. This subgroup in addition lacks the key conserved Tyr residue which acts as a proton donor during catalysis, and no protease activity has been detected to date for Asp f2.
119351	GH18_chitolectin_chitotriosidase	1.99e-12	358	513	170	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
0.0	1	947	1	947
2.07e-236	59	947	3	1049
1.48e-227	61	819	5	915
9.37e-159	289	755	35	508
2.10e-132	1	513	209	835

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.98e-10	281	513	98	350	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
5.29e-10	281	513	98	350	Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]
5.90e-09	357	513	166	334	Crystal structure of signalling protein from sheep(SPS-40) at 3.0A resolution using crystal grown in the presence of polysaccharides [Ovis aries],1ZBK_A Recognition of specific peptide sequences by signalling protein from sheep mammary gland (SPS-40): Crystal structure of the complex of SPS-40 with a peptide Trp-Pro-Trp at 2.9A resolution [Ovis aries],1ZL1_A Crystal structure of the complex of signalling protein from sheep (SPS-40) with a designed peptide Trp-His-Trp reveals significance of Asn79 and Trp191 in the complex formation [Ovis aries],2DPE_A Crystal structure of a secretory 40KDA glycoprotein from sheep at 2.0A resolution [Ovis aries],2DSU_A Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution [Ovis aries],2DSV_A Interactions of protective signalling factor with chitin-like polysaccharide: Crystal structure of the complex between signalling protein from sheep (SPS-40) and a hexasaccharide at 2.5A resolution [Ovis aries],2DSW_A Binding of chitin-like polysaccharides to protective signalling factor: crystal structure of the complex of signalling protein from sheep (SPS-40) with a pentasaccharide at 2.8 A resolution [Ovis aries],2FDM_A Crystal structure of the ternary complex of signalling glycoprotein frm sheep (SPS-40)with hexasaccharide (NAG6) and peptide Trp-Pro-Trp at 3.0A resolution [Ovis aries],2G41_A Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution [Ovis aries],2G8Z_A Crystal structure of the ternary complex of signalling protein from sheep (SPS-40) with trimer and designed peptide at 2.5A resolution [Ovis aries]
5.90e-09	357	513	166	334	Crystal structure of signalling protein from goat SPG-40 in the presense of N,N',N''-triacetyl-chitotriose at 2.6A resolution [Capra hircus]
7.84e-09	357	513	166	334	Crystal Structure of the goat signalling protein (SPG-40) complexed with a designed peptide Trp-Pro-Trp at 3.2A resolution [Capra hircus],1ZBW_A Crystal structure of the complex formed between signalling protein from goat mammary gland (SPG-40) and a tripeptide Trp-Pro-Trp at 2.8A resolution [Capra hircus],1ZU8_A Crystal structure of the goat signalling protein with a bound trisaccharide reveals that Trp78 reduces the carbohydrate binding site to half [Capra hircus],2AOS_A Protein-protein Interactions of protective signalling factor: Crystal structure of ternary complex involving signalling protein from goat (SPG-40), tetrasaccharide and a tripeptide Trp-pro-Trp at 2.9 A resolution [Capra hircus],2B31_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel [Capra hircus],2DSZ_A Three dimensional structure of a goat signalling protein secreted during involution [Capra hircus],2DT0_A Crystal structure of the complex of goat signalling protein with the trimer of N-acetylglucosamine at 2.45A resolution [Capra hircus],2DT1_A Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09 A Resolution [Capra hircus],2DT2_A Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 2.9A resolution [Capra hircus],2DT3_A Crystal structure of the complex formed between goat signalling protein and the hexasaccharide at 2.28 A resolution [Capra hircus],2O92_A Crystal structure of a signalling protein (SPG-40) complex with tetrasaccharide at 3.0A resolution [Capra hircus],2OLH_A Crystal structure of a signalling protein (SPG-40) complex with cellobiose at 2.78 A resolution [Capra hircus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.16e-56	61	555	193	752	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
6.17e-09	357	513	187	356	Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2
3.04e-08	357	513	166	334	Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1
3.36e-08	357	513	187	356	Chitinase-3-like protein 1 OS=Capra hircus OX=9925 GN=CHI3L1 PE=1 SV=1
4.46e-08	357	513	187	356	Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000018	0.000020

TMHMM Annotations help

There is no transmembrane helices in An12g05330-T-p1.

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