logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: SDRG_14915-t26_1-p1

You are here: Home > Sequence: SDRG_14915-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 Saprolegnia diclina
Lineage Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
CAZyme ID SDRG_14915-t26_1-p1
CAZy Family GT2|GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
307 JH767211|CGC1 32868.62 9.2148
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SdiclinaVS20 17448 1156394 89 17359
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in SDRG_14915-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 46 293 9.6e-28 0.9058823529411765

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
173825 ascorbate_peroxidase 3.66e-28 51 297 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 2.50e-21 51 295 34 243
L-ascorbate peroxidase
166005 PLN02364 3.49e-15 51 295 36 246
L-ascorbate peroxidase 1
173827 secretory_peroxidase 1.10e-14 48 295 33 282
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.
178467 PLN02879 4.96e-14 51 295 37 246
L-ascorbate peroxidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.30e-17 23 295 14 246
2.29e-17 23 295 13 244
6.02e-17 23 295 12 243
1.12e-16 23 295 12 243
2.14e-16 23 303 12 252

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.00e-16 22 295 12 245
CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE [Pisum sativum],1APX_B CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE [Pisum sativum],1APX_C CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE [Pisum sativum],1APX_D CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE [Pisum sativum]
4.82e-16 102 299 85 262
Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
6.43e-16 102 299 85 262
Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
6.60e-16 102 299 85 262
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]
6.69e-16 102 299 86 263
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
2.02e-16 18 295 9 246
L-ascorbate peroxidase 1, cytosolic OS=Oryza sativa subsp. indica OX=39946 GN=APX1 PE=2 SV=1
3.42e-16 51 295 34 243
L-ascorbate peroxidase 3 OS=Arabidopsis thaliana OX=3702 GN=APX3 PE=1 SV=1
5.24e-16 22 295 13 246
L-ascorbate peroxidase, cytosolic OS=Pisum sativum OX=3888 GN=APX1 PE=1 SV=2
6.61e-15 18 295 9 246
L-ascorbate peroxidase 1, cytosolic OS=Oryza sativa subsp. japonica OX=39947 GN=APX1 PE=1 SV=1
1.50e-14 51 296 116 345
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

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000219 0.999741 CS pos: 19-20. Pr: 0.9796

TMHMM  Annotations      help

There is no transmembrane helices in SDRG_14915-t26_1-p1.