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CAZyme Information: VDB84094.1

You are here: Home > Sequence: VDB84094.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Blumeria graminis
Lineage Ascomycota; Leotiomycetes; ; Erysiphaceae; Blumeria; Blumeria graminis
CAZyme ID VDB84094.1
CAZy Family GH47
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
470 52498.62 6.8065
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_BgraminisTritici96224 8470 1268274 123 8347
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 20 420 3.7e-52 0.9594594594594594

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395573 Glyco_hydro_18 3.89e-60 20 412 1 307
Glycosyl hydrolases family 18.
214753 Glyco_18 5.92e-41 20 412 1 334
Glyco_18 domain.
119349 GH18_chitinase-like 3.98e-39 22 204 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 3.41e-37 47 246 54 262
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.
225862 ChiA 1.40e-30 14 425 33 435
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 470 1 470
1.10e-180 7 433 9 435
1.10e-180 1 433 2 435
1.33e-175 6 427 7 429
8.25e-133 20 425 34 440

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.42e-20 77 248 91 266
Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568]
6.37e-20 77 248 86 261
Crystal structure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6.48e-20 77 248 83 258
Structural and thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
6.65e-20 77 248 86 261
Crystal Structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
6.82e-20 77 248 89 264
Structure of Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.66e-15 77 215 153 292
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
8.47e-15 80 250 123 297
Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
8.47e-15 80 250 123 297
Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
8.47e-15 80 250 123 297
Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
5.56e-13 65 291 77 302
Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.022710 0.977251 CS pos: 19-20. Pr: 0.9347

TMHMM  Annotations      help

There is no transmembrane helices in VDB84094.1.