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CAZyme Information: POW19348.1

You are here: Home > Sequence: POW19348.1

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 Puccinia striiformis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
CAZyme ID POW19348.1
CAZy Family GH63
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A2S4WC67]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
493 53727.79 7.7284
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2 14629 N/A 0 14629
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in POW19348.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 224 475 1.7e-30 0.6182432432432432

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395573 Glyco_hydro_18 1.21e-29 123 475 4 303
Glycosyl hydrolases family 18.
214753 Glyco_18 1.88e-29 238 475 122 330
Glyco_18 domain.
225862 ChiA 4.92e-28 227 487 179 431
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119365 GH18_chitinase 1.54e-26 227 473 137 316
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.
119351 GH18_chitolectin_chitotriosidase 1.29e-24 232 471 124 333
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
4.99e-177 86 493 1 420
5.51e-66 295 491 1 198
1.78e-46 124 493 29 407
3.45e-43 230 472 94 336
8.69e-40 116 488 39 395

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.33e-15 219 475 155 373
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]
1.03e-14 219 475 406 624
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]
1.31e-13 227 474 135 403
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]
1.31e-13 227 474 135 403
Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone [Serratia marcescens],1UR9_B Interactions of a family 18 chitinase with the designed inhibitor HM508, and its degradation product, chitobiono-delta-lactone [Serratia marcescens]
1.77e-13 230 485 178 412
Chain A, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.61e-12 230 485 210 444
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
3.69e-12 227 474 135 403
Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
7.50e-12 185 470 96 346
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
7.82e-12 247 470 170 357
Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3
7.54e-11 247 470 161 348
Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999850 0.000173

TMHMM  Annotations      help

There is no transmembrane helices in POW19348.1.