CAZyme Information: OJD20706.1

Basic Information

• Species: Blastomyces percursus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces percursus
• CAZyme ID: OJD20706.1
• CAZy Family: CE4
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1J9PXR6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
257		28386.90	4.2510

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BpercursusEI222	10384	N/A	99	10285

• Gene Location: location=LGTZ01001741:220-1090(+)

Full Sequence      

MDWEYPGGNGVDYKQIPNSEKEWEIDAYPLMLAELRSALGHDQIISAAVPGLPRDMLAFT
PATLPSILESIDFFNIMTYDLMNLRDNVTKHHTGLSLSLQSIDAYQTAGIPPSKANFGFA
FYVRWFRTEKPETGSGCEKNPTGCKTVLLEDLETGESTGQAGTFSWNKPAPSQVAASFER
ALAGGTYDEFVPACNGADKEENIWWTWDTETIKMKMQPIMVARGVGGAFAWELGEDGPEF
TRLQALTEGLREIGTVE

Enzyme Prediction     

EC	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	1	237	3.1e-33	0.6148648648648649

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	1.63e-39	1	236	110	307	Glycosyl hydrolases family 18.
214753	Glyco_18	2.57e-30	1	236	113	334	Glyco_18 domain.
119365	GH18_chitinase	1.30e-22	1	236	131	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.
119351	GH18_chitolectin_chitotriosidase	2.30e-16	1	233	118	338	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.
225862	ChiA	2.08e-15	2	250	174	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS65584.1|GH18	3.27e-153	1	257	118	385
QSS55345.1|GH18	3.41e-150	1	257	147	414
EAA66094.1|GH18	6.09e-104	1	250	105	351
CAE7199879.1|GH18	1.86e-102	1	249	136	382
QKX61480.1|GH18	1.60e-101	1	253	126	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	3.10e-08	1	135	123	263	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	3.26e-07	1	135	123	263	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1E9L_A	4.25e-07	1	236	116	344	The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]
5GZU_A	4.35e-07	1	203	155	361	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
5GZT_B	4.55e-07	1	203	406	612	Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O35744|CHIL3_MOUSE	2.26e-06	1	236	137	365	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2
sp|H2A0L4|CHI1_PINMG	5.92e-06	1	252	140	380	Putative chitinase 1 OS=Margaritifera margaritifera OX=102329 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

There is no transmembrane helices in OJD20706.1.