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CAZyme Information: PHYSODRAFT_354823-t26_1-p1

You are here: Home > Sequence: PHYSODRAFT_354823-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phytophthora sojae
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
CAZyme ID PHYSODRAFT_354823-t26_1-p1
CAZy Family GH3
CAZyme Description heme peroxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
338 37520.66 9.2785
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PsojaeP6497 28142 1094619 1653 26489
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PHYSODRAFT_354823-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 69 322 1.4e-59 0.9607843137254902

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 1.21e-145 57 326 4 253
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.
178218 PLN02608 2.97e-77 85 330 32 251
L-ascorbate peroxidase
173823 plant_peroxidase_like 5.70e-64 67 320 1 255
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.
166005 PLN02364 1.25e-61 84 322 33 246
L-ascorbate peroxidase 1
178467 PLN02879 5.05e-61 80 322 30 246
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.10e-207 1 338 1 342
1.36e-96 48 329 79 368
7.78e-95 67 327 97 350
8.32e-94 58 329 79 342
1.90e-89 15 325 40 352

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.01e-77 59 324 1 260
Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major]
1.05e-77 58 324 1 261
The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
1.35e-77 59 324 1 260
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
1.43e-77 59 324 1 260
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
3.36e-76 58 324 1 261
The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.45e-93 67 335 100 362
Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1
3.96e-90 65 329 86 348
Cytochrome c peroxidase, mitochondrial OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=ccp-1 PE=3 SV=1
3.80e-89 58 338 105 384
Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1
1.64e-86 68 327 92 343
Cytochrome c peroxidase, mitochondrial OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=CCP1 PE=3 SV=1
5.23e-86 77 327 106 348
Cytochrome c peroxidase, mitochondrial OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CCP1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999797 0.000247

TMHMM  Annotations      help

There is no transmembrane helices in PHYSODRAFT_354823-t26_1-p1.