CAZyme Information: QRD03396.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRD03396.1
• CAZy Family: GH47
• CAZyme Description: peroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314		33325.77	7.6021

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069037:512056-513052(-)

Full Sequence      

MYPSSLLLLASSAAAFSLPDVSAILPLFSRESGGSSCPSKWNDISKELTSKFLSDGQCNP
DARAAIRLIFHECGSWNKAQGAKGGCDGSLILSSEELLRSENKGLEGIAGYIKDRANFYQ
TSVADMIVFAGNHAVVTCPGGPVVKTFVGRKDSTTAAPDGLLPDVNAPAADLFKLFQDKG
FNEVDLAALLGAHSTSNQFNFNTTDGAKGQPQDSTPGVWDVKYYAETLNAPKGVVVFPSD
IKLAAHPTVGKEFKGFVNNQGKWNGKFADAMGRMALFGSGTTDGKGLIDCTGALPRATNA
KREMRAMPMFACRH

Enzyme Prediction     

No EC number prediction in QRD03396.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	42	278	3.2e-53	0.984313725490196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	3.17e-88	41	308	17	301	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	7.53e-32	54	274	10	253	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	1.45e-27	35	274	9	278	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.
395089	peroxidase	7.97e-27	44	194	1	150	Peroxidase.
173825	ascorbate_peroxidase	2.19e-22	51	279	22	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD03396.1|AA2	6.41e-232	1	314	1	314
QDS74803.1|AA2	7.19e-120	8	308	6	304
AUS45858.1|AA2	2.11e-85	9	294	13	299
QDS77202.1|AA2	8.90e-81	34	295	28	287
QDS68272.1|AA2	4.04e-76	37	306	152	415

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ABQ_A	4.60e-35	44	295	20	283	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-SS. MUTATED RESIDUES T2K, A49C, A61C, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R,A309K AND A314R. [Pleurotus eryngii]
6ISS_A	3.68e-33	33	297	17	299	Chain A, Ligninase H8 [Phanerochaete chrysosporium RP-78],6ISS_G Chain G, Ligninase H8 [Phanerochaete chrysosporium RP-78]
5ABN_A	1.32e-32	44	295	20	283	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi. MUTATED RESIDUES D69S, T70D, S86E, D146T, Q202L, H232E, Q239R AND S301K. [Pleurotus eryngii]
5ABO_A	1.84e-32	44	295	20	283	CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi-br. MUTATED RESIDUES T2K, D69S, T70D, S86E, A131K, D146T, Q202L, Q219K, H232E, Q239R, L288R, S301K, A308R, A309K AND A314R. [Pleurotus eryngii]
2VKA_A	3.78e-32	44	295	20	283	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UR19|VPL1_PLEER	1.65e-30	44	295	50	313	Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
sp|O94753|VPL2_PLEER	3.18e-30	44	295	50	313	Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1
sp|P21764|LIG3_PHACH	1.41e-29	35	297	41	320	Ligninase LG3 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG3 PE=2 SV=1
sp|P06181|LIG8_PHACH	1.96e-29	33	297	38	320	Ligninase H8 OS=Phanerodontia chrysosporium OX=2822231 GN=LPOA PE=1 SV=1
sp|P49012|LIG2_PHACH	5.14e-29	33	295	38	318	Ligninase LG2 OS=Phanerodontia chrysosporium OX=2822231 GN=GLG2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.649598	0.350416

TMHMM  Annotations     

There is no transmembrane helices in QRD03396.1.