CAZyme Information: QRD00736.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRD00736.1
• CAZy Family: GH18
• CAZyme Description: chitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
415		46040.34	5.9103

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069033:618691-619987(+)

Full Sequence      

MVNTTMALLIGLSFWLLLMAAAAAAEPPFLTQGKLRWIMYLTGQHNVVPEYPMETMLRGV
THVTLAFMRSDIFNDANRTEWPLFTTVDEVRPKFNNGTRVQVAIGGWGDTAGFEKGAKTE
KSRKLFASNVKAMLEATGADGIDMDWEYPGGNGEDYKVNPNSSKVWEITAFPELLAAVRA
AVGPLMTISAAVPGLERDMLAFTPATIPRIMESIDFLNVMTYDMMNRRDNVTKHHAGTQQ
SLAAIKAYRKRGVPADRLNVGTAFYVKWFKTANGKDCSAQATGCPTELMEDPKTGADLGK
AGAFSWHDQVPSELSNSFDKALKHGVCDRESGGCTYWDADERLFWSWESKDTIYRKLRVV
IGEMKLEGAFAWGLGEDAPEFEHLSGANHGISDEEISRSSKIDAMRNAARWRNEL

Enzyme Prediction     

EC	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	53	381	4.3e-47	0.8648648648648649

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	1.30e-62	36	377	1	307	Glycosyl hydrolases family 18.
214753	Glyco_18	7.45e-41	38	377	3	334	Glyco_18 domain.
119349	GH18_chitinase-like	5.28e-34	38	224	2	178	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.
119365	GH18_chitinase	8.81e-34	99	377	86	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	1.74e-28	61	283	29	263	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
QRD00736.1|GH18	7.40e-314	1	415	1	415
CBY01085.1|GH18	4.69e-168	35	391	1	354
EAA66094.1|GH18	3.02e-158	39	406	1	366
AEO67798.1|GH18	6.77e-157	22	393	22	391
AEO60157.1|GH18	2.58e-152	14	388	7	378

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KST_A	7.86e-20	51	283	24	282	Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KST_B Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KXL_A Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXL_B Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KXN_A	7.86e-20	51	283	24	282	Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KXM_A	3.57e-19	51	283	24	282	Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXM_B Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
5GZU_A	7.14e-19	61	382	51	382	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	7.90e-19	61	382	302	633	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|Q9D7Q1|CHIT1_MOUSE	1.21e-15	11	309	9	312	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|P36909|CHIT_STRLI	1.68e-15	84	338	319	590	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
sp|Q13231|CHIT1_HUMAN	3.89e-15	37	286	31	290	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|A6N6J0|CHI46_TRIHA	1.08e-14	52	407	57	427	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
sp|P11220|CHIT_STRPL	2.20e-14	99	338	334	591	Chitinase 63 OS=Streptomyces plicatus OX=1922 GN=chtA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000448	0.999542	CS pos: 25-26. Pr: 0.6688

TMHMM  Annotations     

Start	End
7	29