CAZyme Information: KGB77350.3

Basic Information

• Species: Cryptococcus gattii VGII
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGII
• CAZyme ID: KGB77350.3
• CAZy Family: GH3
• CAZyme Description: endochitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
519	CP025759|CGC6	54445.76	4.0537

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiVGIIR265	6705	294750	281	6424

• Gene Location: location=CP025759:733539-735363(-)

Full Sequence      

MYFVGSTTLFAILTALAVRSAPAPQSGADYTCDSDTQWHDAYQTVTCPGDTVCVTGASGN
PCQFPSGYGQSAIMAAAVTSASAAGGVTSATAAGGISVTGTGTTGGEAAASSSSGAAVTT
ARSAVASSASHTNSAASPSGTSISNGASGSNRFVTYWDNYANMGGINAAQLTAVTHVILS
FADMTNWATDQTTWQFMESSDGNFDSSTAATLKGMQSGLKVCGALGGWGLDSVMATAIRG
GDSSIATFVANVKGFADYFDLDGIDIDWEFPVASDDANLITFVTQLRAALGDDKLISIAL
GARVDTTDAAAFNSDTFSKLDGLVDMWNVMTYDYVNRYSTTTEQQAGNRVVTTVMDYYER
QGITMEKCNVGFPMNAKYFTLTETCDSSNPIGCSLPGRDYYEDNGVDNYKSGWVRFNAGL
DSTLGTKGTEWATKMRAQWEARPTDGSTEITADVSNAWVDETNNVFWTWLSDSDMKTTCQ
NWVTTGKVGGAMVWSLNQDDKGQDGGSHMAALAACIQES

Enzyme Prediction     

No EC number prediction in KGB77350.3.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	151	505	5.1e-47	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	2.24e-41	152	499	1	307	Glycosyl hydrolases family 18.
214753	Glyco_18	1.30e-32	154	499	3	334	Glyco_18 domain.
119349	GH18_chitinase-like	4.80e-31	153	333	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.
119365	GH18_chitinase	1.08e-27	153	374	4	261	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.
119351	GH18_chitolectin_chitotriosidase	1.91e-25	175	500	29	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
KGB77350.3|GH18	0.0	1	519	1	519
UOH83768.1|GH18	4.05e-307	1	519	1	530
AAW46130.2|GH18	9.39e-304	1	519	1	531
AFR94094.2|GH18	4.97e-301	1	519	1	530
AUB23701.1|GH18	4.97e-301	1	519	1	530

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YBT_A	9.00e-14	175	500	35	349	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
3FXY_A	1.30e-13	175	500	31	345	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
6TSB_AAA	1.95e-13	212	407	84	286	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	2.20e-13	212	407	103	305	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
1W9P_A	4.91e-13	139	504	31	394	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q95M17|CHIA_BOVIN	2.99e-13	175	500	52	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q873X9|CHIB1_ASPFM	2.52e-12	139	504	31	394	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1
sp|E9QRF2|CHIB1_ASPFU	2.52e-12	139	504	31	394	Endochitinase B1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chiB1 PE=3 SV=1
sp|Q9BZP6|CHIA_HUMAN	2.92e-12	212	500	83	366	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	3.69e-11	175	500	52	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000234	0.999761	CS pos: 20-21. Pr: 0.9721

TMHMM  Annotations     

There is no transmembrane helices in KGB77350.3.