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CAZyme Information: PGTG_03208-t26_1-p1

You are here: Home > Sequence: PGTG_03208-t26_1-p1

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 Puccinia graminis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
CAZyme ID PGTG_03208-t26_1-p1
CAZy Family CE5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
423 47402.45 5.8921
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PgraminisCRL75-36-700-3 16309 418459 509 15800
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 35 397 1.4e-31 0.918918918918919

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 6.51e-33 36 397 1 329
Glyco_18 domain.
395573 Glyco_hydro_18 1.92e-31 36 397 1 302
Glycosyl hydrolases family 18.
119351 GH18_chitolectin_chitotriosidase 4.03e-29 101 394 70 333
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.
225862 ChiA 6.97e-23 101 412 126 433
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119365 GH18_chitinase 1.62e-22 37 396 1 316
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.11e-58 37 410 37 414
3.58e-36 85 394 22 335
3.02e-33 34 401 37 405
1.31e-32 93 404 80 395
7.09e-32 53 401 93 441

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.69e-19 101 401 157 447
Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
3.31e-18 52 397 15 350
Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
6.61e-16 101 408 122 412
Chain A, Glycosyl Hydrolase [Niallia circulans]
6.20e-14 109 393 88 350
Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]
6.20e-14 109 393 88 350
Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.20e-15 101 408 154 444
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
3.71e-12 101 393 95 366
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
4.05e-12 102 393 88 346
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
7.16e-12 93 414 79 366
Class V chitinase OS=Arabidopsis thaliana OX=3702 GN=ChiC PE=1 SV=1
2.42e-11 75 393 56 351
Oviduct-specific glycoprotein OS=Mus musculus OX=10090 GN=Ovgp1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000241 0.999738 CS pos: 20-21. Pr: 0.9787

TMHMM  Annotations      help

There is no transmembrane helices in PGTG_03208-t26_1-p1.