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CAZyme Information: QYA_121587T0-p1

You are here: Home > Sequence: QYA_121587T0-p1

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 Mucor lusitanicus
Lineage Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor lusitanicus
CAZyme ID QYA_121587T0-p1
CAZy Family CE9
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A168H2G1]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
272 30974.02 5.9367
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MlusitanicusCBS277-49 11852 747725 0 11852
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:12

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 1 236 7.1e-17 0.6418918918918919

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119356 GH18_hevamine_XipI_class_III 6.99e-80 1 272 3 263
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.
395573 Glyco_hydro_18 1.47e-11 1 236 2 220
Glycosyl hydrolases family 18.
119349 GH18_chitinase-like 5.40e-08 1 197 1 177
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
119363 GH18_CTS3_chitinase 5.90e-07 68 272 69 251
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
119350 GH18_chitinase_D-like 8.63e-06 63 200 65 197
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.07e-50 1 272 30 287
5.22e-50 1 272 27 285
5.22e-50 1 272 27 285
5.22e-50 1 272 27 285
5.22e-50 1 272 27 285

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.66e-45 1 272 8 264
ScCTS1_apo crystal structure [Saccharomyces cerevisiae],2UY3_A ScCTS1_8-chlorotheophylline crystal structure [Saccharomyces cerevisiae],2UY4_A ScCTS1_acetazolamide crystal structure [Saccharomyces cerevisiae],2UY5_A ScCTS1_kinetin crystal structure [Saccharomyces cerevisiae],4TXE_A ScCTS1 in complex with compound 5 [Saccharomyces cerevisiae]
7.66e-45 1 272 3 257
Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_B Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_C Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_D Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum]
4.34e-40 1 272 3 255
CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR [Hevea brasiliensis],1LLO_A Chain A, HEVAMINE [Hevea brasiliensis],2HVM_A Hevamine A At 1.8 Angstrom Resolution [Hevea brasiliensis]
5.80e-40 1 272 3 253
cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala]
2.59e-38 1 272 3 255
Chain A, Hevamine A [Hevea brasiliensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.98e-46 1 272 31 292
Chitinase 1 OS=Rhizopus oligosporus OX=4847 GN=CHI1 PE=1 SV=1
2.04e-46 1 272 31 292
Chitinase 2 OS=Rhizopus oligosporus OX=4847 GN=CHI2 PE=1 SV=1
2.92e-46 1 272 25 287
Chitinase 3 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT3 PE=1 SV=2
3.04e-45 1 272 28 277
Acidic endochitinase SE2 OS=Beta vulgaris OX=161934 GN=SE2 PE=1 SV=1
3.11e-44 1 272 20 270
Chitinase 1 OS=Candida albicans OX=5476 GN=CHT1 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000021 0.000006

TMHMM  Annotations      help

There is no transmembrane helices in QYA_121587T0-p1.