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CAZyme Information: HVAS_10078920.1-p1

You are here: Home > Sequence: HVAS_10078920.1-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 Hemileia vastatrix
Lineage Basidiomycota; Pucciniomycetes; ; Zaghouaniaceae; Hemileia; Hemileia vastatrix
CAZyme ID HVAS_10078920.1-p1
CAZy Family GH18
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
271 31473.39 9.0026
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_HvastatrixRaceXXXIII 12854 N/A 284 12570
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 1 122 1.3e-31 0.4627450980392157

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 4.14e-92 1 211 33 251
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 1.52e-52 1 209 34 243
L-ascorbate peroxidase
173823 plant_peroxidase_like 1.27e-49 1 207 21 255
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 1.48e-44 1 209 36 246
L-ascorbate peroxidase 1
178467 PLN02879 2.40e-43 1 209 37 246
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.02e-80 1 228 128 374
8.49e-80 1 227 117 362
8.49e-80 1 227 117 362
8.49e-80 1 227 117 362
8.49e-80 1 227 117 362

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.17e-54 1 228 46 291
Chain A, Cytochrome C Peroxidase [Saccharomyces cerevisiae]
1.48e-53 1 209 29 258
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
1.97e-53 1 209 29 258
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
2.09e-53 1 209 29 258
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]
2.15e-53 1 209 30 259
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
5.45e-79 1 226 121 365
Cytochrome c peroxidase, mitochondrial OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=ccp1 PE=3 SV=1
8.74e-77 1 228 139 393
Cytochrome c peroxidase, mitochondrial OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP1 PE=3 SV=1
2.41e-76 1 226 116 360
Cytochrome c peroxidase, mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ccp1 PE=3 SV=1
6.25e-76 1 211 113 343
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
1.25e-75 1 228 110 357
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999974 0.000073

TMHMM  Annotations      help

There is no transmembrane helices in HVAS_10078920.1-p1.