logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: KFA52867.1

You are here: Home > Sequence: KFA52867.1

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 Stachybotrys chartarum
Lineage Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
CAZyme ID KFA52867.1
CAZy Family GH32
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
416 KL651051|CGC1 46559.54 9.1905
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SchartarumIBT40293 11453 1280524 0 11453
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KFA52867.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 99 348 4.4e-53 0.9921568627450981

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173826 ligninase 4.82e-103 96 365 14 291
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 4.31e-30 102 344 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 6.96e-26 125 348 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 5.62e-21 125 324 20 185
Peroxidase.
178218 PLN02608 1.06e-20 125 347 35 243
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.84e-138 45 415 129 499
4.06e-138 45 415 131 501
4.06e-138 45 415 131 501
4.06e-138 45 415 131 501
7.90e-138 45 415 164 534

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.93e-34 94 362 13 290
CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM1_B CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM I [Pleurotus ostreatus],4BM2_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Ii [Pleurotus ostreatus],4BM3_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iii [Pleurotus ostreatus],4BM4_A Crystal Structure Of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form Iv [Pleurotus ostreatus]
8.58e-30 96 362 22 297
Chain A, Peroxidase [Coprinopsis cinerea],1LY8_B Chain B, Peroxidase [Coprinopsis cinerea]
3.45e-29 95 292 13 202
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]
4.76e-29 95 292 13 202
Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii],5FNB_B Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Septuple Mutant E37k, H39r, V160a, T184m, Q202l, D213a & G330r [Pleurotus eryngii]
5.89e-29 96 362 22 297
Chain A, Peroxidase [Coprinopsis cinerea],1LYK_B Chain B, Peroxidase [Coprinopsis cinerea]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.24e-28 96 362 42 317
Peroxidase OS=Coprinopsis cinerea OX=5346 GN=CIP1 PE=1 SV=2
5.93e-28 96 362 43 318
Peroxidase OS=Arthromyces ramosus OX=5451 PE=1 SV=3
1.10e-27 96 362 42 317
Peroxidase OS=Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) OX=240176 GN=CIP1 PE=3 SV=1
1.47e-27 95 291 43 231
Versatile peroxidase VPL1 OS=Pleurotus eryngii OX=5323 GN=vpl1 PE=1 SV=1
3.82e-27 95 291 43 231
Versatile peroxidase VPL2 OS=Pleurotus eryngii OX=5323 GN=vpl2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001202 0.998770 CS pos: 19-20. Pr: 0.9336

TMHMM  Annotations      help

There is no transmembrane helices in KFA52867.1.