CAZyme Information: mRNA_M_BR32_EuGene_00007941-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00007941-p1
• CAZy Family: AA12
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
507		55122.97	6.7557

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PoryzaeBR32	14781	N/A	432	14349

• Gene Location: location=BR32_scaffold00001:2349683-2351346(-)

Full Sequence      

MLHRLFFLTPLLLRWSVLAAPMPDAVDSALAKRDMICFDAPTRTVTVTVDGNGQPQNTPA
PVDPVTHIASIIIPSGTSPASSPAGTAKAQSSQTVIATPSQTSGASNPSPSAANWSGYRS
VLYFTNWGIYGANYQPQDLPVDTVTHILYSFANIATDGEVISSDTYSDIDKHYPTDSWND
LGRNAYGCVKQLYLLKKKNRHLKVLLSIGGWTWSPKFAPIAATAAGRNRFATSAVKLLAD
WGLDGLDIDWEYPTNKNEADNYVLLLKACREALDAYSAKNAQGYKFLLTVATPAGPENYG
NMNLEGMDKFVDFWNLMAYDYAGSWDTTTGHQSNLYLDDQNKVATKFSTEKAVQDYFARG
IDAAKITLGLPLYGRSFASTGGLGKPFSGLGDGSIERGVWLYKDLPRPGAIVAYDNVAKA
SYSYDAAKREFVTYDTVDSAREKTRYMKQKGLGGAVFWEASGDRKGDQSLVGTVARGVGL
DVLDKSTNLLAYPVSQYDNIRNGMPGV

Enzyme Prediction     

No EC number prediction in mRNA_M_BR32_EuGene_00007941-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	118	470	5.3e-81	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119365	GH18_chitinase	6.67e-134	123	463	4	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	1.53e-121	119	463	1	334	Glyco_18 domain.
225862	ChiA	2.39e-93	118	482	38	440	Chitinase, GH18 family [Carbohydrate transport and metabolism].
395573	Glyco_hydro_18	1.52e-92	119	463	1	307	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	4.84e-86	121	458	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ56002.1|GH18	0.0	1	496	1	496
VBB72338.1|GH18	2.09e-192	17	505	19	501
EAA36073.3|GH18	6.90e-192	116	505	37	424
AEO70479.1|GH18	7.14e-188	118	506	102	489
CDP23242.1|GH18	1.72e-177	17	505	19	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1D2K_A	2.50e-167	117	505	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	7.13e-167	117	505	2	391	Chain A, CHITINASE 1 [Coccidioides immitis],1LL7_B Chain B, CHITINASE 1 [Coccidioides immitis]
1LL6_A	1.43e-166	117	505	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	1.21e-163	116	504	3	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]
1W9P_A	1.59e-163	116	504	41	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q1E3R8|CHI1_COCIM	1.90e-167	106	505	26	426	Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
sp|C5P230|CHI1_COCP7	2.69e-167	106	505	26	426	Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
sp|P0CB51|CHI1_COCPS	2.69e-167	108	505	28	426	Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
sp|E9ERT9|CHI1_METRA	3.43e-167	117	504	38	423	Endochitinase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chit1 PE=3 SV=1
sp|Q873X9|CHIB1_ASPFM	8.18e-163	116	504	41	431	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000413	0.999556	CS pos: 19-20. Pr: 0.9762

TMHMM  Annotations     

There is no transmembrane helices in mRNA_M_BR32_EuGene_00007941-p1.