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CAZyme Information: PUG3_T010134-RA-p1

You are here: Home > Sequence: PUG3_T010134-RA-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 Globisporangium ultimum
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
CAZyme ID PUG3_T010134-RA-p1
CAZy Family GH63
CAZyme Description Cytochrome c peroxidase, mitochondrial
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
240 27577.33 4.9734
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GultimumBR650 14086 1223559 0 14086
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in PUG3_T010134-RA-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 36 220 2.4e-41 0.7137254901960784

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 3.09e-105 5 224 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 6.77e-60 37 224 79 247
L-ascorbate peroxidase
173823 plant_peroxidase_like 4.95e-43 26 218 55 255
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.
178467 PLN02879 1.47e-40 37 220 82 246
L-ascorbate peroxidase
166005 PLN02364 1.88e-37 37 220 81 246
L-ascorbate peroxidase 1

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.05e-125 1 236 57 340
1.79e-71 37 226 162 351
1.08e-69 38 234 154 349
1.75e-69 37 225 179 366
4.06e-69 37 234 167 360

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.06e-59 33 222 72 261
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]
1.45e-59 33 222 71 260
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]
1.94e-59 33 222 71 260
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
2.05e-59 33 222 71 260
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
2.11e-59 33 222 72 261
The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.52e-69 37 234 167 362
Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1
4.34e-68 37 234 161 357
Cytochrome c peroxidase, mitochondrial OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CCP1 PE=3 SV=1
1.63e-67 37 221 185 368
Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1
2.46e-66 37 234 156 352
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
4.92e-66 37 234 159 353
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000062 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in PUG3_T010134-RA-p1.