CAZyme Information: CGB_K3410C-t26_1-p1

Basic Information

• Species: Cryptococcus gattii VGI
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGI
• CAZyme ID: CGB_K3410C-t26_1-p1
• CAZy Family: GT39
• CAZyme Description: endochitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
501	CP000296|CGC5	53366.79	4.6799

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiWM276	6580	367775	15	6565

• Gene Location: location=CP000296:736941-738694(-)

Full Sequence      

MYFPLLPNLGPITLAIATHSGMMHTRQLLALAIPFVSLVPVEILANFHQVAVAVTSASAA
GGVTSATVAGGISVTGTGTTGGEAAASSSSRAAVTTARSAVASSASHTNSAASPSGTSTS
NGASGSNRFVTYWDNYANMGGVNAAQLTTVTHVILSTLLTHLIVIAFADMTNWATKQTTW
QFMESSDGNFGSSTAATLKGMQSGLKVCGALGGWGLDSVMVTAVRGGDSSIATFVANVKG
FADYFNLDGIDIDWEFPSASDDANLITFVTQLRAALGDDKLISIALGARVDTTDAAAFNS
DTFSKLDGLVDMWNVMTYDYVNRYSTATEQQAGNRVVTTVMDYYEKQGITMEKCNVGFPM
NAKYFTLTETCDSSNPIGCSLPGREYYEDNGVDNYKSGWVRFNPGLDSTLGTKGTEWATK
MRTQWEARPADGSTEITADVSNAWVDETNNVFWTWLSDFDMKKTCQNWVTSGKVGGAMVW
SLNQVIISIHSIVYAQMLIHF

Enzyme Prediction     

No EC number prediction in CGB_K3410C-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	127	484	8.6e-46	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395573	Glyco_hydro_18	4.81e-37	128	484	1	306	Glycosyl hydrolases family 18.
214753	Glyco_18	1.89e-32	130	484	3	333	Glyco_18 domain.
119349	GH18_chitinase-like	6.84e-28	129	319	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	3.85e-27	129	360	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	4.63e-26	157	482	26	338	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
ADV25006.1|GH18	0.0	1	501	1	501
KGB77350.3|GH18	4.90e-261	51	484	75	498
AAW46130.2|GH18	4.83e-238	55	484	92	510
UOH83768.1|GH18	3.81e-237	126	484	161	509
AFR94094.2|GH18	5.40e-237	126	484	161	509

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	1.79e-14	198	390	84	291	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	2.04e-14	198	390	103	310	Chain AAA, Peroxiredoxin [Clostridioides difficile 630]
2YBT_A	4.71e-14	198	483	66	346	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	6.84e-14	198	483	62	342	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]
6G9C_A	1.29e-12	199	483	97	371	Crystal structure of immunomodulatory active chitinase from Trichuris suis, TsES1 [Trichuris suis],6G9C_B Crystal structure of immunomodulatory active chitinase from Trichuris suis, TsES1 [Trichuris suis],6G9E_A Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_B Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_C Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_D Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_E Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis],6G9E_F Crystal structure of immunomodulatory active chitinase from Trichuris suis - TsES1 - 6 molecules in ASU [Trichuris suis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q95M17|CHIA_BOVIN	2.08e-13	158	483	50	363	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9BZP6|CHIA_HUMAN	3.72e-13	198	483	83	363	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q9W092|CHIT2_DROME	8.60e-12	158	483	69	387	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	1.47e-11	198	483	83	363	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q6RY07|CHIA_RAT	2.59e-11	198	483	83	363	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.932304	0.067694

TMHMM  Annotations     

There is no transmembrane helices in CGB_K3410C-t26_1-p1.