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CAZyme Information: THC89244.1

You are here: Home > Sequence: THC89244.1

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 tanneri
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
CAZyme ID THC89244.1
CAZy Family AA7
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A4V6RQN7]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
993 107509.48 4.4729
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AtanneriNIH1004 13590 N/A 33 13557
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 302 585 1e-38 0.7432432432432432

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119357 GH18_zymocin_alpha 1.29e-145 293 581 58 345
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 7.71e-42 302 580 73 333
Glyco_18 domain.
395573 Glyco_hydro_18 1.71e-34 302 579 70 305
Glycosyl hydrolases family 18.
119351 GH18_chitolectin_chitotriosidase 6.09e-30 293 580 60 340
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 1.51e-24 302 469 91 266
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 1 964 240 1236
0.0 1 964 241 1228
0.0 1 964 233 1212
0.0 1 965 242 1227
0.0 1 964 287 1320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.64e-19 303 621 77 386
Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
2.59e-18 287 590 66 359
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
4.57e-18 303 621 77 386
Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
2.65e-17 287 590 66 359
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
3.02e-17 293 590 73 360
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.32e-83 63 632 191 751
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
2.62e-18 303 583 97 367
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
3.48e-18 303 583 97 367
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
3.28e-16 303 583 97 367
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
8.11e-16 288 584 74 368
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
1.000062 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in THC89244.1.