CAZyme Information: HVAS_10010713.1-p1

Basic Information

• Species: Hemileia vastatrix
• Lineage: Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix
• CAZyme ID: HVAS_10010713.1-p1
• CAZy Family: AA5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
184	PHNK01001071|CGC1	19726.00	7.7928

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HvastatrixRaceXXXIII	12854	N/A	284	12570

• Gene Location: location=PHNK01001071:17542-18581(-)

Full Sequence      

MLTSVVKSLDYAAGSWSPKTGSQSAFVANCPTGEAPISFQTGVAKLIQQGFKPSQIVAGI
PAYAHSWTLTQPKLQVSHFGNISTSIFQNHTDKTPPGGKADDKPGVDNCGNKTTWGGTWL
VSEMIDRGFLAKDEMSGGNGYKRYFDACSDTPYLTNGQTFFSYDDSQSSRLKAQFVAAHQ
LGGV

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	8	184	5.4e-19	0.40202702702702703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.21e-18	1	184	168	326	Glyco_18 domain.
119365	GH18_chitinase	1.01e-16	5	184	197	314	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.
225862	ChiA	3.96e-15	2	184	236	415	Chitinase, GH18 family [Carbohydrate transport and metabolism].
395573	Glyco_hydro_18	4.64e-15	2	184	160	299	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	9.06e-10	14	184	192	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	3.14e-49	14	184	228	398
ALL41259.1|GH18	3.05e-40	14	184	7	178
ALL40920.1|GH18	1.32e-35	59	184	2	127
CDR43393.1|GH18	5.82e-26	13	184	213	385
CRX79101.1|GH18	2.42e-21	13	184	163	335

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6INX_A	5.57e-10	37	184	211	321	Structural insights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A	2.82e-08	2	183	218	368	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	2.91e-08	2	183	469	619	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]
1OGB_A	3.16e-06	46	184	275	400	Chitinase b from Serratia marcescens mutant D142N [Serratia marcescens],1OGB_B Chitinase b from Serratia marcescens mutant D142N [Serratia marcescens],1OGG_A chitinase b from serratia marcescens mutant d142n in complex with inhibitor allosamidin [Serratia marcescens],1OGG_B chitinase b from serratia marcescens mutant d142n in complex with inhibitor allosamidin [Serratia marcescens]
6JK9_A	3.16e-06	46	184	273	398	Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-14 [Serratia marcescens],6JK9_B Crystal structure of Serratia marcescens Chitinase B complexed with compound 2-8-14 [Serratia marcescens],7C34_A Crystal structure of Serratia marcescens Chitinase B complexed with Berberine [Serratia marcescens],7C34_B Crystal structure of Serratia marcescens Chitinase B complexed with Berberine [Serratia marcescens]

Swiss-Prot Hits     

HVAS_10010713.1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000005

TMHMM  Annotations     

There is no transmembrane helices in HVAS_10010713.1-p1.