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CAZyme Information: PTTG_06474-t43_1-p1

You are here: Home > Sequence: PTTG_06474-t43_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 triticina
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
CAZyme ID PTTG_06474-t43_1-p1
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
410 44875.89 8.9558
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1 15692 630390 814 14878
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PTTG_06474-t43_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 36 402 2.5e-44 0.9222972972972973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 1.27e-54 39 401 4 330
Glyco_18 domain.
395573 Glyco_hydro_18 8.73e-51 39 401 4 303
Glycosyl hydrolases family 18.
119365 GH18_chitinase 1.83e-49 39 399 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.
225862 ChiA 5.71e-45 35 404 38 422
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 8.27e-40 101 397 66 333
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.63e-301 1 409 1 410
4.17e-71 31 404 20 392
2.05e-64 64 398 6 336
1.46e-61 221 409 1 190
2.40e-51 38 404 29 388

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.77e-33 45 409 56 410
Chain A, Glycosyl Hydrolase [Niallia circulans]
5.14e-30 36 401 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]
5.77e-30 36 401 278 624
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]
1.14e-26 60 398 32 341
Chain A, Probable endochitinase [Caenorhabditis elegans]
1.58e-26 60 398 31 340
Chain A, Probable endochitinase [Caenorhabditis elegans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.25e-31 45 409 88 442
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
4.60e-25 60 398 83 392
Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
1.67e-24 76 400 61 403
Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
1.12e-23 101 396 89 354
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
4.23e-23 98 396 84 346
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000347 0.999609 CS pos: 24-25. Pr: 0.9802

TMHMM  Annotations      help

There is no transmembrane helices in PTTG_06474-t43_1-p1.