CAZyme Information: OJD19524.1

Basic Information

• Species: Emergomyces pasteurianus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces pasteurianus
• CAZyme ID: OJD19524.1
• CAZy Family: GT50
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1J9QUI1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
398		43442.14	5.7061

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EpasteurianusEp9510	9078	1447872	128	8950

• Gene Location: location=LGRN01000008:29997-31512(-)

Full Sequence      

MAYANSSLFVESPPGEYTPFTPISEIRASFANGTKLLIAIGGLGDTKGFSAGAKDDASRK
KYAKNVADMVNKHGFDGVDIDWQYPSGNGQDHKDIPNSEKASEVESFPLLLKEIKNTIGT
GKQLSIAVPGKKSDMIAYTPEKGPEIWEAVDFVNVIMSYDLVNRRDNATAHHTSVKGCLE
TIQNYLGIKLPPEKINLGFAFYAKFFALDPKTNCPFDRPVGCPLVRAELENGTDAGTSGI
VAFESAQVSPPPVPIGVSPNMTCGPLNGFRCKDELCCSSAGFCGHLPEYCSSGCQPHYGK
CDGVDVGSSFRRAQANGMTDMEQGGRYYVDHEAKLFWTWETTDLIARKFEEIVSEKKLGG
VMAWALGLDSYDWSRVGAMQKGMEEYQGREGKKKPSCW

Enzyme Prediction     

EC	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	27	371	9.9e-46	0.7804054054054054

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	2.58e-61	1	369	33	307	Glycosyl hydrolases family 18.
214753	Glyco_18	3.05e-43	33	369	66	334	Glyco_18 domain.
119365	GH18_chitinase	1.68e-38	35	202	86	262	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.
119349	GH18_chitinase-like	8.85e-33	27	162	58	179	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.
119351	GH18_chitolectin_chitotriosidase	3.31e-30	35	213	72	255	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS57709.1|CBM18|GH18	2.87e-235	1	393	46	437
QSS67261.1|CBM18|GH18	3.70e-234	1	393	46	459
QSS66279.1|CBM18|GH18	1.50e-223	1	393	62	466
CAP85554.1|CBM18|GH18	2.51e-145	1	384	42	422
QQK48241.1|CBM18|GH18	1.10e-144	1	384	46	426

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	5.33e-16	35	212	92	271	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	6.08e-16	35	212	111	290	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6JM7_A	6.34e-16	15	215	61	264	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5GZU_A	1.44e-15	35	204	111	285	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	1.57e-15	35	204	362	536	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|A6N6J0|CHI46_TRIHA	7.46e-13	33	206	122	298	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
sp|P32470|CHI1_APHAL	9.72e-13	35	217	123	308	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
sp|P48827|CHI42_TRIHA	1.30e-12	33	206	121	297	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
sp|Q5AM60|CHI4_CANAL	4.81e-12	35	222	103	286	Chitinase 4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT4 PE=3 SV=1
sp|E9ERT9|CHI1_METRA	5.53e-12	35	216	124	308	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000042	0.000000

TMHMM  Annotations     

There is no transmembrane helices in OJD19524.1.