Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna27591.1-v1.0-hybrid |
Family | AA2 |
Protein Properties | Length: 356 Molecular Weight: 38572.6 Isoelectric Point: 5.4144 |
Chromosome | Chromosome/Scaffold: 2 Start: 1521220 End: 1523757 |
Description | Peroxidase superfamily protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 53 | 317 | 0 |
SIVRKQLKKVFKEDIGQAAGLLRLHFHDCFVQGCDGSVLLDGSASGPSEQQAPPNLSLRAKAFQIINDLREIVHSKCGRVVSCADLTALAARDAVFLSGG PEYEVPLGRKDGLNFATRNETLANLPAPTSNTTKLLTDLAKKNLDATDVVALSGGHTIGLGHCTSFTGRLYPTQDASMDKTFANDLKQVCPAADTNATTV LDIRSPDTFDNKYYVDLMNRQGLFTSDQDLYTDKRTRDIVTSFAVNQTLFFEKFVHSMIKMGQLS |
Full Sequence |
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Protein Sequence Length: 356 Download |
MASTFASLCS LLLIVSSVLV SSYFGVSEAQ PSVPVVKGLS WSFYDSSCPK LDSIVRKQLK 60 KVFKEDIGQA AGLLRLHFHD CFVQGCDGSV LLDGSASGPS EQQAPPNLSL RAKAFQIIND 120 LREIVHSKCG RVVSCADLTA LAARDAVFLS GGPEYEVPLG RKDGLNFATR NETLANLPAP 180 TSNTTKLLTD LAKKNLDATD VVALSGGHTI GLGHCTSFTG RLYPTQDASM DKTFANDLKQ 240 VCPAADTNAT TVLDIRSPDT FDNKYYVDLM NRQGLFTSDQ DLYTDKRTRD IVTSFAVNQT 300 LFFEKFVHSM IKMGQLSVLT GSKGEIRANC SMRNSDNANY LSSVVEEDEE SLSEF* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 6.0e-13 | 55 | 318 | 279 | + 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. | ||
cd00314 | plant_peroxidase_like | 1.0e-28 | 53 | 315 | 291 | + 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. | ||
pfam00141 | peroxidase | 6.0e-60 | 55 | 212 | 158 | + Peroxidase. | ||
PLN03030 | PLN03030 | 3.0e-73 | 37 | 334 | 310 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 3.0e-161 | 38 | 331 | 300 | + 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 | 1bgp_A | 0 | 29 | 334 | 1 | 305 | A Chain A, Crystal Structure Of Barley Grain Peroxidase 1 |
PDB | 3hdl_A | 0 | 39 | 335 | 2 | 304 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 1qgj_B | 0 | 39 | 335 | 2 | 300 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1qgj_A | 0 | 39 | 335 | 2 | 300 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1qo4_A | 0 | 39 | 334 | 3 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase N |