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CAZyme Information: KIW05112.1

You are here: Home > Sequence: KIW05112.1

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 Verruconis gallopava
Lineage Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
CAZyme ID KIW05112.1
CAZy Family GH47
CAZyme Description Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A0D1YWP1]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
426 46913.08 4.4177
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_VgallopavaCBS43764 9871 N/A 53 9818
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:25

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 35 384 8.8e-80 0.9459459459459459

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214753 Glyco_18 2.34e-130 36 381 1 334
Glyco_18 domain.
119365 GH18_chitinase 2.07e-129 37 381 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.
395573 Glyco_hydro_18 1.34e-95 36 381 1 307
Glycosyl hydrolases family 18.
225862 ChiA 2.17e-90 33 392 36 432
Chitinase, GH18 family [Carbohydrate transport and metabolism].
119351 GH18_chitolectin_chitotriosidase 6.97e-83 38 376 2 336
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
1.36e-214 32 426 35 429
5.71e-203 23 426 47 443
3.47e-197 17 422 13 424
5.73e-197 35 426 8 399
7.25e-197 18 422 28 425

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.38e-195 32 423 2 393
Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus]
2.10e-194 32 423 40 431
Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9P_B Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9U_A Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9U_B Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9V_A Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],1W9V_B Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],2A3A_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3A_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3B_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3B_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3C_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3C_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3E_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2A3E_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2IUZ_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],2IUZ_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],3CH9_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CH9_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CHC_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHC_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHD_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHD_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHE_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHE_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHF_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus],3CHF_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus]
2.49e-192 29 423 10 403
Crystal structure of Aspergillus niger chitinase B [Aspergillus niger]
6.57e-181 35 424 3 391
Chain A, CHITINASE 1 [Coccidioides immitis],1LL4_A Chain A, Chitinase 1 [Coccidioides immitis],1LL4_B Chain B, Chitinase 1 [Coccidioides immitis],1LL4_C Chain C, Chitinase 1 [Coccidioides immitis],1LL4_D Chain D, Chitinase 1 [Coccidioides immitis]
1.88e-180 35 424 3 391
Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.08e-193 32 423 40 431
Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
1.08e-193 32 423 40 431
Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
1.23e-186 35 424 4 396
Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1
1.23e-186 35 424 4 396
Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
1.76e-181 5 424 3 426
Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000226 0.999747 CS pos: 24-25. Pr: 0.8333

TMHMM  Annotations      help

There is no transmembrane helices in KIW05112.1.