CAZyme Information: HCAG_06565-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_06565-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: endochitinase 1 precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597		65524.46	7.1178

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476660:765317-767801(+)

Full Sequence      

MTHPPIQCQLPCAGKRDRDHDHNHPAASHRRGLFIKQLPCCRSLAWCFVALLWFTALSSV
SAAPGCRPSVNVLPFKDDVDDYNKIDCVSVLRSTVWATSTTTITLLFPSASSSASASSFS
AATSTPAADYPVISQTSESTTPRPYEGSCRVRPTRPTHKPPSPSSPIPSLPSVYPTRPSP
PSPSPSHNMSSPDGYKSIVYYVNWAIYARNYNPQDLPVKKLTHVLYAFANVRAESGEVFL
TDTWADTDKHFPTDSWSETGNNVYGCVKQLFLLKKQNRHLKVLLSIGGWTYSPHFGAAVS
TPAARTKFAESATQLLLNLGFDGLDVDWEYPKDDEEAKNLVELLKTTREVLDRAGGKDRR
FLLTVACPAGRQNFEKLRLAEMTPYLDFYNLMAYDYSGSWDTIAGHQSNIEPSKSNPKST
PFSTKEAVDYYLGVGNVPPSKLILGMPLYGRTFADTDGPGTPFHGDGGQGSFEKGIWDYK
SLPKVGAVEYIDSLEKGGCGASWSYDSSSRTMISYDNVAMVEEKTKYIIQKGLGGGMWWE
SSGDRDPRNGDKANGSLIGTFVEGVGGKLETSENALSYPESKYDNLRAGFPNGTTQH

Enzyme Prediction     

EC	3.2.1.14:25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	195	549	3.5e-78	0.9527027027027027

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119365	GH18_chitinase	8.90e-127	197	544	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.
214753	Glyco_18	1.96e-123	196	544	1	334	Glyco_18 domain.
225862	ChiA	5.66e-89	193	570	36	441	Chitinase, GH18 family [Carbohydrate transport and metabolism].
395573	Glyco_hydro_18	2.39e-87	196	544	1	307	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	7.41e-74	200	539	4	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS59996.1|GH18	0.0	1	597	27	623
QSS68432.1|GH18	0.0	1	597	27	621
QSS49927.1|GH18	0.0	1	597	27	621
AAF80370.1|GH18|3.2.1.14	0.0	35	597	1	560
AAF80371.1|GH18	1.78e-233	189	591	1	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1D2K_A	1.38e-161	194	591	2	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]
1LL7_A	3.93e-161	194	591	2	391	Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis]
1LL6_A	7.89e-161	194	591	2	391	Chain A, CHITINASE 1 [Coccidioides immitis],1LL6_B Chain B, CHITINASE 1 [Coccidioides immitis],1LL6_C Chain C, CHITINASE 1 [Coccidioides immitis],1LL6_D Chain D, CHITINASE 1 [Coccidioides immitis]
1WNO_A	1.06e-156	194	589	4	392	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]
1W9P_A	1.38e-156	194	589	42	430	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|Q92222|CHIB_EMEND	2.15e-184	194	591	3	396	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
sp|G5EAZ3|CHIB1_EMENI	2.15e-184	194	591	3	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
sp|P0CB51|CHI1_COCPS	2.41e-160	194	591	37	426	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
sp|Q1E3R8|CHI1_COCIM	2.41e-160	194	591	37	426	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
sp|C5P230|CHI1_COCP7	5.52e-159	194	591	37	426	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.898490	0.101497

TMHMM  Annotations     

There is no transmembrane helices in HCAG_06565-t26_1-p1.