CAZyme Information: POW13168.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW13168.1
• CAZy Family: GH7|GH7|GH7
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
404	PKSL01000026|CGC1	43479.25	8.2897

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93-210	15090	N/A	0	15090

• Gene Location: location=PKSL01000026:302523-304546(+)

Full Sequence      

MRSSSPLLSLSCLLATLLFVNVQAHPSPKVKGYYPTYNAKAQPPSKIDWSAYTDVLFFMV
IPQADFTLAYDPKLTPAEGQKLVTNHVNPLFSTGGWTGSQHFSNLTLTEAGRKKFAKSLV
DFGKKNGFTGIELDWEYANGQGIGCNSRNPADVVNFGLFVKEIRALWPQADLTAAVGITG
LIGADGGAATTTETALLTQNLNYINLMAYDVYGAWAPTTGPLAPLHATCAPAAFGQSVET
GLQVALKQGFKPSQVVLGIPGYAKRLELTSPTLGPTTVSGQSSFYYQNHTTVTPPGGNFD
DKPGKDICGNARAWGGSFLVNELISNGWLSKDQKTGLNGYERHWDACSGQPFLTNGKYLI
TYDDLDSTIAKAKFAKQNQLGGIYFFDTMGPTPATVRAARQAVY

Enzyme Prediction     

No EC number prediction in POW13168.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	29	387	5.1e-49	0.918918918918919

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119365	GH18_chitinase	9.94e-58	32	385	3	316	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.
214753	Glyco_18	2.93e-55	29	387	1	330	Glyco_18 domain.
395573	Glyco_hydro_18	3.87e-52	32	387	4	303	Glycosyl hydrolases family 18.
225862	ChiA	2.83e-50	26	387	36	419	Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351	GH18_chitolectin_chitotriosidase	1.55e-38	88	383	68	333	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
AAP42832.1|GH18	1.32e-225	1	403	1	418
CDR43393.1|GH18	5.19e-74	27	404	23	406
ALL41259.1|GH18	1.57e-71	207	403	1	198
CRX79101.1|GH18	2.10e-69	89	384	41	336
AEH16745.1|GH18|3.2.1.14	8.35e-55	33	403	47	398

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ITX_A	6.44e-36	81	402	117	417	Chain A, Glycosyl Hydrolase [Niallia circulans]
5GZU_A	8.35e-30	29	387	27	373	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	9.35e-30	29	387	278	624	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]
6BT9_A	4.27e-28	86	390	157	447	Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
3WD0_A	5.77e-27	53	386	49	407	Serratia marcescens Chitinase B, tetragonal form [Serratia marcescens],3WD1_A Serratia marcescens Chitinase B complexed with syn-triazole inhibitor [Serratia marcescens],3WD2_A Serratia marcescens Chitinase B complexed with azide inhibitor [Serratia marcescens],3WD3_A Serratia marcescens Chitinase B complexed with azide inhibitor [Serratia marcescens],3WD4_A Serratia marcescens Chitinase B complexed with azide inhibitor and quinoline compound [Serratia marcescens],4Z2G_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 26 [Serratia marcescens],4Z2H_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 29 [Serratia marcescens],4Z2I_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 30 [Serratia marcescens],4Z2J_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 31 [Serratia marcescens],4Z2K_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 32 [Serratia marcescens],4Z2L_A Serratia marcescens Chitinase B complexed with macrolide inhibitor 33 [Serratia marcescens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P20533|CHIA1_NIACI	4.73e-34	81	402	149	449	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
sp|P11797|CHIB_SERMA	2.88e-26	53	386	45	403	Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
sp|Q11174|CHIT_CAEEL	5.66e-25	53	384	83	392	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	2.93e-22	78	382	81	354	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	5.29e-22	67	401	68	381	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000255	0.999723	CS pos: 24-25. Pr: 0.9791

TMHMM  Annotations     

There is no transmembrane helices in POW13168.1.