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CAZyme Information: HCBG_00208-t26_1-p1

You are here: Home > Sequence: HCBG_00208-t26_1-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 Histoplasma capsulatum
Lineage Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
CAZyme ID HCBG_00208-t26_1-p1
CAZy Family AA1
CAZyme Description bacteriodes thetaiotaomicron symbiotic chitinase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1045 GG663363|CGC2 113356.15 7.3130
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_HcapsulatumG186AR 9364 447093 110 9254
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 153 282 3.2e-19 0.35135135135135137

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119351 GH18_chitolectin_chitotriosidase 1.58e-54 55 292 30 353
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.
214753 Glyco_18 8.31e-53 55 283 28 333
Glyco_18 domain.
395573 Glyco_hydro_18 1.43e-48 55 282 25 305
Glycosyl hydrolases family 18.
119365 GH18_chitinase 5.24e-36 55 282 28 320
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.
119349 GH18_chitinase-like 2.30e-29 55 186 26 158
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 73 1045 1 1055
0.0 55 1045 161 1143
3.73e-119 55 638 24 609
1.83e-114 49 636 146 726
4.69e-67 55 434 160 603

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.30e-25 55 292 33 354
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]
6.47e-24 55 292 33 354
Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
8.14e-24 55 283 32 341
High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
8.27e-24 55 283 32 341
Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
8.27e-24 55 283 32 341
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
1.13e-22 15 283 2 362
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
9.04e-22 55 303 53 385
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
9.12e-22 55 283 53 364
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
6.34e-21 43 283 39 360
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
8.21e-21 55 283 51 354
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000005 0.000032

TMHMM  Annotations      help

There is no transmembrane helices in HCBG_00208-t26_1-p1.