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CAZyme Information: KEF58311.1

You are here: Home > Sequence: KEF58311.1

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 Exophiala aquamarina
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
CAZyme ID KEF58311.1
CAZy Family GH32
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A072PEQ5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
643 AMGV01000004|CGC31 69361.29 4.1743
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918 13118 1182545 0 13118
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KEF58311.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 269 636 3.9e-61 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 7.53e-57 269 632 1 334
Glyco_18 domain.
395573 Glyco_hydro_18 3.87e-48 269 632 1 307
Glycosyl hydrolases family 18.
119365 GH18_chitinase 9.48e-45 270 632 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.
225862 ChiA 5.43e-43 270 634 40 425
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 1.33e-38 282 635 18 342
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.20e-41 270 639 158 531
5.76e-41 270 639 124 497
1.08e-40 270 639 124 497
7.15e-39 266 635 49 425
7.81e-38 282 640 16 379

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.50e-37 284 642 14 365
Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
2.71e-29 285 635 29 360
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]
6.72e-29 285 635 29 360
Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
1.62e-28 285 635 47 378
Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]
1.66e-28 285 635 29 360
Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.56e-25 285 635 45 376
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
3.75e-25 332 643 155 449
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
1.40e-24 282 635 41 362
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
3.67e-22 272 635 32 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
9.28e-22 282 635 41 366
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000372 0.999608 CS pos: 16-17. Pr: 0.9659

TMHMM  Annotations      help

There is no transmembrane helices in KEF58311.1.