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CAZyme Information: I303_00654-t42_1-p1

You are here: Home > Sequence: I303_00654-t42_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 Kwoniella dejecticola
Lineage Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella dejecticola
CAZyme ID I303_00654-t42_1-p1
CAZy Family AA5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
601 KI894027|CGC18 61296.32 4.3571
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_KdejecticolaCBS10117 8724 1296121 122 8602
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in I303_00654-t42_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 228 587 9.4e-41 0.9527027027027027

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 3.97e-41 230 581 3 334
Glyco_18 domain.
395573 Glyco_hydro_18 1.33e-39 228 581 1 307
Glycosyl hydrolases family 18.
119349 GH18_chitinase-like 4.03e-29 229 417 1 177
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 2.94e-25 230 581 2 322
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 1.59e-23 230 581 2 341
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
1.73e-127 1 601 1 531
7.43e-123 49 599 27 517
7.26e-120 230 601 165 530
7.26e-120 230 601 165 530
1.44e-119 230 601 165 530

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.64e-10 277 582 85 374
Crystal structure of immunomodulatory active chitinase from Trichuris suis, TsES1 [Trichuris suis],6G9C_B Crystal structure of immunomodulatory active chitinase from Trichuris suis, TsES1 [Trichuris suis],6G9E_A Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_B Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_C Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_D Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_E Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_F Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis]
1.28e-09 286 516 101 347
Chain A, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
1.36e-09 251 582 31 343
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1.37e-09 251 582 31 343
Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
2.08e-09 286 583 81 385
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.00e-10 232 582 27 366
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
1.72e-08 251 582 52 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
2.04e-08 286 484 115 312
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
7.20e-08 286 582 111 390
Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
3.47e-07 286 584 121 392
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000279 0.999689 CS pos: 30-31. Pr: 0.6666

TMHMM  Annotations      download full data without filtering help

Start End
7 29