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CAZyme Information: GAQ09750.1

You are here: Home > Sequence: GAQ09750.1

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 Aspergillus lentulus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
CAZyme ID GAQ09750.1
CAZy Family GH55
CAZyme Description killer toxin subunits alpha/beta
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1386 BCLY01000012|CGC3 149086.27 4.4933
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AlentulusIFM54703 9916 N/A 259 9657
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:3 3.2.1.14:3 3.2.1.14:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 400 768 1e-46 0.9493243243243243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 0.0 400 763 1 345
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.
214753 Glyco_18 3.16e-54 400 762 1 333
Glyco_18 domain.
395573 Glyco_hydro_18 7.37e-46 400 761 1 305
Glycosyl hydrolases family 18.
119351 GH18_chitolectin_chitotriosidase 2.61e-36 429 762 29 340
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.
119365 GH18_chitinase 9.13e-36 401 651 1 266
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 5 1384 117 1473
0.0 3 1384 114 1480
0.0 5 1384 109 1458
0.0 2 1384 118 1488
0.0 9 1384 185 1528

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.31e-21 399 765 1 338
Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_B Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_C Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_D Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJW_A Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJW_B Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJX_A Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_B Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_C Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_D Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1NWR_A Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_B Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_C Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_D Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWS_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWT_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWU_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],7CJ2_A Chain A, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens],7CJ2_B Chain B, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens]
5.69e-21 399 765 1 337
Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution [Capra hircus]
5.69e-21 399 765 1 337
Crystal structure of a 40 kDa signalling protein from Porcine (SPP-40) at 2.89A resolution [Sus scrofa],1XRV_A Crystal Structure of the novel secretory signalling protein from Porcine (SPP-40) at 2.1A resolution. [Sus scrofa],1ZB5_A Recognition of peptide ligands by signalling protein from porcine mammary gland (SPP-40): Crystal structure of the complex of SPP-40 with a peptide Trp-Pro-Trp at 2.45A resolution [Sus scrofa],1ZBC_A Crystal Structure of the porcine signalling protein liganded with the peptide Trp-Pro-Trp (WPW) at 2.3 A resolution [Sus scrofa]
7.98e-21 402 765 4 344
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
8.09e-21 402 765 4 344
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
4.37e-100 112 767 134 716
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
6.76e-21 397 765 20 359
Chitinase-3-like protein 1 OS=Homo sapiens OX=9606 GN=CHI3L1 PE=1 SV=2
6.76e-21 390 778 13 367
Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2
3.95e-20 390 765 13 359
Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3
4.27e-20 429 765 52 367
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000061 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in GAQ09750.1.