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CAZyme Information: CNK00840-t26_1-p1

You are here: Home > Sequence: CNK00840-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 Cryptococcus neoformans
Lineage Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
CAZyme ID CNK00840-t26_1-p1
CAZy Family GT3
CAZyme Description endochitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
531 AE017351.1|CGC4 55532.55 3.8813
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CneoformansJEC21 7004 214684 372 6632
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in CNK00840-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 163 517 3.7e-46 0.956081081081081

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395573 Glyco_hydro_18 1.16e-41 164 511 1 307
Glycosyl hydrolases family 18.
214753 Glyco_18 1.23e-33 166 511 3 334
Glyco_18 domain.
119349 GH18_chitinase-like 1.20e-31 165 345 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 5.19e-27 165 386 4 261
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 2.09e-26 187 512 29 342
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
0.0 1 531 1 531
3.72e-313 1 531 1 530
5.58e-308 1 531 1 530
5.58e-308 1 531 1 530
1.67e-304 1 531 1 519

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.95e-15 187 512 35 349
Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
1.02e-14 187 512 31 345
Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
1.12e-13 164 512 2 343
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1.13e-13 164 512 2 343
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]
2.68e-13 164 512 2 343
Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.78e-13 187 512 52 366
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
3.18e-13 224 512 83 366
Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
2.24e-12 164 512 23 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
3.51e-12 164 531 44 407
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
3.51e-12 164 531 44 407
Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000198 0.999778 CS pos: 20-21. Pr: 0.9816

TMHMM  Annotations      help

There is no transmembrane helices in CNK00840-t26_1-p1.