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CAZyme Information: EEU36943.1

You are here: Home > Sequence: EEU36943.1

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 Fusarium vanettenii
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
CAZyme ID EEU36943.1
CAZy Family CE8
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:C7ZGN3]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1530 GG698925|CGC2 169466.35 4.6197
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Fvanettenii77134 15708 660122 0 15708
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EEU36943.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 159 516 3.7e-68 0.9662162162162162

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 9.07e-83 161 508 1 334
Glyco_18 domain.
119357 GH18_zymocin_alpha 2.00e-75 163 508 3 345
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.
119351 GH18_chitolectin_chitotriosidase 6.62e-70 162 508 1 341
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.
395573 Glyco_hydro_18 1.63e-68 161 508 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 1.67e-66 162 508 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 1 1530 1 1499
0.0 54 1479 76 1529
0.0 61 1526 81 1572
0.0 59 1523 53 1527
0.0 59 1523 53 1518

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.04e-46 160 508 4 350
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
4.59e-45 160 508 4 350
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
2.31e-44 162 528 95 458
Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
2.71e-44 162 632 4 449
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]
6.50e-44 180 508 22 342
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.96e-42 162 508 24 365
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
2.70e-42 162 508 24 365
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
4.29e-42 180 508 43 363
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
4.42e-42 162 508 24 357
Chitinase-3-like protein 1 OS=Capra hircus OX=9925 GN=CHI3L1 PE=1 SV=1
4.92e-42 162 508 24 365
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000543 0.999425 CS pos: 30-31. Pr: 0.9689

TMHMM  Annotations      download full data without filtering help

Start End
12 34