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CAZyme Information: ATY61069.1

You are here: Home > Sequence: ATY61069.1

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 Cordyceps militaris
Lineage Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
CAZyme ID ATY61069.1
CAZy Family GH132
CAZyme Description glycoside hydrolase family 18
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
764 CP023323|CGC22 85226.93 6.9881
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CmilitarisATCC34164 9362 N/A 75 9287
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ATY61069.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 106 449 6.1e-75 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 1.39e-92 108 447 1 334
Glyco_18 domain.
119357 GH18_zymocin_alpha 4.09e-91 110 447 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 1.13e-84 109 448 1 342
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.
395573 Glyco_hydro_18 5.06e-77 108 447 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 4.17e-67 109 447 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 1 764 1 764
2.47e-241 3 763 49 1490
8.28e-229 3 461 49 508
8.28e-229 3 461 49 508
8.28e-229 3 461 49 508

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.97e-51 104 448 1 351
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5.08e-50 104 448 1 351
Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
9.99e-48 106 448 1 343
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]
1.98e-47 108 448 2 343
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
2.03e-47 108 448 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.89e-48 109 448 24 366
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
6.68e-47 109 448 24 366
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
5.85e-46 108 448 23 366
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
9.71e-46 102 448 17 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
1.55e-44 129 448 45 362
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.982610 0.017414

TMHMM  Annotations      help

There is no transmembrane helices in ATY61069.1.