CAZyme Information: mRNA_M_BR32_EuGene_00125141-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00125141-p1
• CAZy Family: GH92
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
254	BR32_scaffold00022|CGC1	26858.42	5.7811

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_scaffold00022:22321-23395(+)

Full Sequence      

MLASLSSSSLLVASLLFVTAPVPVNGNKLCNPWKPVVADLKASFKGCNADARMAMRAAFH
DCFPGSCDGSLILANECNDRPDDNGPLVPICETLAQKAIDFKVGTADLIQAAGVVAITSC
AGPRTYFYVGRKDSSVPSPEGQLPNSESTAQQQIDACKAKGFTTTDLVAMVGAHSAGVSQ
QGLSFDSTPEKLDSTVFYPETASEKGPTSLQSDYALSNDTQTKTAWKNMGRSNALWRAQF
VTTIMAVRCITTST

Enzyme Prediction     

No EC number prediction in mRNA_M_BR32_EuGene_00125141-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	37	244	4.4e-40	0.9450980392156862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	1.46e-40	18	240	1	263	Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
395089	peroxidase	1.17e-29	59	232	24	187	Peroxidase.
173823	plant_peroxidase_like	7.23e-29	59	243	26	249	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
173827	secretory_peroxidase	1.55e-17	59	241	41	272	Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.
178218	PLN02608	5.62e-14	98	219	75	211	L-ascorbate peroxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ64256.1|AA2	1.07e-175	1	247	1	247
CAE7013403.1|AA2	3.24e-45	33	241	29	241
CAE7196231.1|AA2	9.35e-37	33	241	77	292
QDS75494.1|AA2	1.26e-35	19	240	105	334
QCC62988.1|AA2	1.45e-34	33	241	61	275

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LY8_A	2.81e-24	27	240	19	272	Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
1LYK_A	7.26e-23	27	233	19	265	Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]
1ARP_A	7.35e-23	27	233	20	266	Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 angstroms resolution: structural comparisons with the lignin and cytochrome C peroxidases [Penicillium janthinellum],1ARU_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARV_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARW_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARX_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1ARY_A Crystal Structures Of Cyanide-And Triiodide-Bound Forms Of Arthromyces Ramosus Peroxidase At Different Ph Values. Perturbations Of Active Site Residues And Their Implication In Enzyme Catalysis [Agaricales sp. 'Arthromyces ramosus'],1C8I_A BINDING MODE OF HYDROXYLAMINE TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1CK6_A BINDING MODE OF SALICYLHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZA_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1GZB_A PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],1HSR_A BINDING MODE OF BENZHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE [Agaricales sp. 'Arthromyces ramosus'],2E39_A Crystal structure of the CN-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3A_A Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus'],2E3B_A Crystal structure of the HA-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution [Agaricales sp. 'Arthromyces ramosus']
1H3J_A	1.31e-21	27	233	18	264	Chain A, PEROXIDASE [Coprinopsis cinerea],1H3J_B Chain B, PEROXIDASE [Coprinopsis cinerea]
3Q3U_A	4.55e-21	27	227	12	251	Trametes cervina lignin peroxidase [Trametopsis cervina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28314|PER_COPCI	4.74e-22	27	233	39	285	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	4.79e-22	27	233	40	286	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|A8NK72|PER_COPC7	3.26e-21	27	233	39	285	Peroxidase OS=Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OX=240176 GN=CIP1 PE=3 SV=1
sp|Q9UVP6|VPS1_PLEER	2.02e-18	27	229	42	284	Versatile peroxidase VPS1 OS=Pleurotus eryngii OX=5323 GN=vps1 PE=1 SV=1
sp|P06181|LIG8_PHACH	6.48e-17	26	228	38	281	Ligninase H8 OS=Phanerodontia chrysosporium OX=2822231 GN=LPOA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000289	0.999685	CS pos: 26-27. Pr: 0.9724

TMHMM  Annotations     

There is no transmembrane helices in mRNA_M_BR32_EuGene_00125141-p1.