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CAZyme Information: M747DRAFT_358420-t43_1-p1

You are here: Home > Sequence: M747DRAFT_358420-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 Aspergillus niger
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
CAZyme ID M747DRAFT_358420-t43_1-p1
CAZy Family GT2
CAZyme Description class V chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1203 135174.41 4.6492
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnigerATCC13496 12468 1353008 274 12194
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 110 454 2.1e-64 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 1.78e-75 111 451 1 334
Glyco_18 domain.
119357 GH18_zymocin_alpha 4.34e-74 113 448 3 342
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
119351 GH18_chitolectin_chitotriosidase 4.87e-67 112 455 1 345
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.
395573 Glyco_hydro_18 5.13e-65 111 451 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 8.30e-52 112 451 1 322
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 19 1059 30 1110
2.54e-263 8 1186 9 1198
4.83e-257 16 1184 20 1166
2.72e-251 11 1190 12 1216
4.13e-248 19 1121 28 1165

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.48e-39 111 455 2 346
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1.52e-39 111 455 2 346
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]
1.52e-39 111 455 2 346
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]
1.55e-39 111 455 2 346
Structure of human chitotriosidase [Homo sapiens]
1.60e-39 111 455 8 363
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.53e-43 9 454 316 715
Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
3.32e-38 104 455 16 367
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
4.83e-37 115 457 27 371
Chitinase-like protein 4 OS=Mus musculus OX=10090 GN=Chil4 PE=1 SV=2
1.40e-36 102 455 15 379
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
6.72e-36 115 457 27 371
Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.988513 0.011543

TMHMM  Annotations      help

There is no transmembrane helices in M747DRAFT_358420-t43_1-p1.