Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna25852.1-v1.0-hybrid |
Family | AA2 |
Protein Properties | Length: 350 Molecular Weight: 37218.5 Isoelectric Point: 4.7497 |
Chromosome | Chromosome/Scaffold: 6 Start: 38178151 End: 38179481 |
Description | Peroxidase superfamily protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 160 | 331 | 1.6e-24 |
GGPDFNVELGRRDGLVSKASRVAGNLPEPSFDLKQLNTMFSKHNLTQTDVIALSGAHTLGFSHCNRFADRLYSFSSSSAVDPSLDPDYAKQLMSACPKDV DPRIAIDMDPRNSTNVDNVYYQNLVAGKGLFTSDEVLFSDSASQSTVVDFANSPGEFSGAFITAMRKLGRVD | |||
AA2 | 8 | 136 | 9.4e-37 |
DAEKDSSDNLSLAGDGFDTVIKAKQAVEAQCPAVVSCADILALAARDVVVLGGGPDFNVELGRRDGLVSKASRVAGNLPEPSFDLKQLNTMFSKHNLTQT DVIALSGAHTLGFSHCNRFADRLYSFSSS |
Full Sequence |
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Protein Sequence Length: 350 Download |
MITSPNGDAE KDSSDNLSLA GDGFDTVIKA KQAVEAQCPA VVSCADILAL AARDVVVLGG 60 GPDFNVELGR RDGLVSKASR VAGNLPEPSF DLKQLNTMFS KHNLTQTDVI ALSGAHTLGF 120 SHCNRFADRL YSFSSSSAVD PSLDPDYAKQ LMSACPKDGG GPDFNVELGR RDGLVSKASR 180 VAGNLPEPSF DLKQLNTMFS KHNLTQTDVI ALSGAHTLGF SHCNRFADRL YSFSSSSAVD 240 PSLDPDYAKQ LMSACPKDVD PRIAIDMDPR NSTNVDNVYY QNLVAGKGLF TSDEVLFSDS 300 ASQSTVVDFA NSPGEFSGAF ITAMRKLGRV DVKTGSEGEI RTDCTAFNS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 0.003 | 281 | 312 | 32 | + Peroxidase. | ||
pfam00141 | peroxidase | 7.0e-16 | 160 | 217 | 58 | + Peroxidase. | ||
pfam00141 | peroxidase | 3.0e-39 | 6 | 117 | 112 | + Peroxidase. | ||
cd00693 | secretory_peroxidase | 5.0e-76 | 3 | 161 | 159 | + 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. | ||
cd00693 | secretory_peroxidase | 4.0e-85 | 160 | 347 | 188 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3hdl_A | 6e-40 | 159 | 349 | 112 | 304 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 3hdl_A | 2e-39 | 3 | 158 | 57 | 211 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 3atj_B | 1e-38 | 159 | 349 | 113 | 307 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 3atj_B | 6e-31 | 10 | 159 | 65 | 214 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 3atj_A | 1e-38 | 159 | 349 | 113 | 307 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
Sequence Alignments (This image is cropped. Click for full image.) |
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