CAZyme Information: EJT75948.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT75948.1
• CAZy Family: GH27
• CAZyme Description: ligninase H2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
429		46447.57	6.5029

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

• Gene Location: location=GL385397:2276122-2277411(-)

Full Sequence      

MRLSLLTAALAASPALAYPGMKSTLGEIHARARGGRGSGGRQASDTEADELLDSNELIGD
LITLDESQLTPVGKRIKHLITGSENPESDETYPRGAWGAVQIPQMGSAACAKDTCCIWKY
IADDMVRAFRGKSGRCTDFARAAVRLGFHDAGGWSKSTGNLGGADGSLVLAPEEILRGEN
RGLEEIVELTRKWHDAYKKYGVGMADLVQWGANVATVVCPLGPRIRSYVGRKDSSVPAPH
DLLPPVTGSADFLIELFENKTIKPHGLTALIGAHTTSQQRFVDPSRAGDPQDSTPGVWDV
KFYKETLGSAPARVFKFASDIVLAKDPRISKEFNEFAGPGGQEHWNEDYAREYIRLSLLG
VFNINDLTECTKALPGRVGAFVAPDQSIMDKYLASKVKMDAYADTLRKGDALGSLISTTW
DWLKSVFGN

Enzyme Prediction     

No EC number prediction in EJT75948.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	120	360	3.5e-52	0.9803921568627451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	1.68e-112	106	400	6	307	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.
173823	plant_peroxidase_like	5.12e-29	121	357	3	254	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.
173825	ascorbate_peroxidase	5.06e-20	144	361	34	250	Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
395089	peroxidase	1.10e-18	121	275	1	150	Peroxidase.
178218	PLN02608	1.33e-13	144	360	35	243	L-ascorbate peroxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCF45286.1|AA2	1.36e-218	1	428	1	418
QBZ59830.1|AA2	1.32e-167	1	417	1	464
QRD06638.1|AA2	1.23e-128	54	393	44	377
UNI21317.1|AA2	6.01e-128	54	398	33	376
VBB71993.1|AA2	7.80e-126	56	377	45	360

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LY8_A	1.66e-32	95	384	4	306	Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
1ARP_A	1.63e-31	93	384	3	307	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']
1LYK_A	5.79e-31	95	384	4	306	Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]
1LY9_A	8.00e-31	95	384	4	306	Chain A, Peroxidase [Coprinopsis cinerea],1LY9_B Chain B, Peroxidase [Coprinopsis cinerea],1LYC_A Chain A, Peroxidase [Coprinopsis cinerea],1LYC_B Chain B, Peroxidase [Coprinopsis cinerea]
1H3J_A	1.03e-29	95	384	3	305	Chain A, PEROXIDASE [Coprinopsis cinerea],1H3J_B Chain B, PEROXIDASE [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28314|PER_COPCI	1.18e-30	93	384	20	326	Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
sp|P28313|PER_ARTRA	1.20e-30	93	384	23	327	Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
sp|A8NK72|PER_COPC7	4.26e-30	93	384	20	326	Peroxidase OS=Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OX=240176 GN=CIP1 PE=3 SV=1
sp|P20013|LIGC_TRAVE	1.02e-26	115	375	41	319	Ligninase C OS=Trametes versicolor OX=5325 PE=1 SV=2
sp|P49012|LIG2_PHACH	3.21e-25	114	375	41	318	Ligninase LG2 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000629	0.999334	CS pos: 17-18. Pr: 0.9659

TMHMM  Annotations     

There is no transmembrane helices in EJT75948.1.