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CAZyme Information: QYA_130546T0-p1

You are here: Home > Sequence: QYA_130546T0-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_130546T0-p1
CAZy Family GH152
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A162QG72]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
317 McirCBS277-49_SC05|CGC2 34222.95 5.5595
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

No EC number prediction in QYA_130546T0-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 7 314 6.9e-61 0.7736486486486487

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119365 GH18_chitinase 1.91e-68 13 312 86 322
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.
214753 Glyco_18 5.35e-68 7 312 62 334
Glyco_18 domain.
395573 Glyco_hydro_18 2.70e-57 2 312 55 307
Glycosyl hydrolases family 18.
225862 ChiA 5.21e-56 13 317 128 429
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 1.20e-55 13 312 72 341
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.47e-118 1 317 55 378
1.69e-117 1 317 88 411
5.90e-115 1 317 82 402
2.01e-112 1 317 81 405
6.06e-81 2 312 69 381

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.33e-47 3 315 49 358
Chain A, Fungal chitinase from Rhizomucor miehei (SeMet-substituted proteins) [Rhizomucor miehei]
2.19e-37 11 313 79 360
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]
5.92e-37 11 313 79 360
Crystal Structure of the Ostrinia furnacalis Group I Chitinase catalytic domain E148Q mutant [Ostrinia furnacalis]
1.60e-36 11 313 79 360
Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2 [Ostrinia furnacalis]
1.94e-36 11 313 97 378
Crystal structure of an insect chitinase from the Asian corn borer, Ostrinia furnacalis [Ostrinia furnacalis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.20e-34 13 317 156 443
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
7.41e-32 13 313 97 376
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
9.88e-28 13 312 113 446
Chitinase ChiA OS=Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) OX=376686 GN=chiA PE=1 SV=1
1.83e-26 13 313 130 400
Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
2.36e-24 13 313 91 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.995682 0.004385

TMHMM  Annotations      help

There is no transmembrane helices in QYA_130546T0-p1.