| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20005261m |
| Family | AA2 |
| Protein Properties | Length: 413 Molecular Weight: 44743.8 Isoelectric Point: 9.1281 |
| Chromosome | Chromosome/Scaffold: 93 Start: 39510 End: 43680 |
| Description | ascorbate peroxidase 3 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 155 | 407 | 0 |
| VRDSISSLLEAADYDDGSYGPLLVRLAWHASGTYDKSSCTGGSNGATMRFPPECEWAANRGLAIARQLLEPVKAAHPWISYADLWTLAGVVAIEDMGGPS VAWRPGREDYSDGSKIVPDGRLPNATLGAKHLRDIFHRMGFDDRDIVALSGAHTLGRCHPDRSGFSGPWTNAPTTFSNLYFQELVNNKWRPKKWDGPLQY EDAKTGTLMMLPTDLALLSDRTFKKYVAQYAKDEEAFFKDFAVAFGKLLELGV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 413 Download |
| MHKIHTPDYR GRAMDKGAGN RRLDRFGIVN LKELDLLYRT AKMATSAPRM LRLGSLLARQ 60 AAPSSLLQQQ FRTFSDNAAA EAAKAAPEAV KADSGSKGKI RGVQALIFGG LGAGMLYGYS 120 LFTSQPPPSG PLAGPPTLPT GTAPKTSTPG DYAAVRDSIS SLLEAADYDD GSYGPLLVRL 180 AWHASGTYDK SSCTGGSNGA TMRFPPECEW AANRGLAIAR QLLEPVKAAH PWISYADLWT 240 LAGVVAIEDM GGPSVAWRPG REDYSDGSKI VPDGRLPNAT LGAKHLRDIF HRMGFDDRDI 300 VALSGAHTLG RCHPDRSGFS GPWTNAPTTF SNLYFQELVN NKWRPKKWDG PLQYEDAKTG 360 TLMMLPTDLA LLSDRTFKKY VAQYAKDEEA FFKDFAVAFG KLLELGVPFP SAE 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 3.0e-60 | 157 | 404 | 259 | + 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. | ||
| PLN02364 | PLN02364 | 7.0e-67 | 174 | 406 | 234 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 8.0e-70 | 174 | 406 | 233 | + L-ascorbate peroxidase | ||
| PLN02608 | PLN02608 | 5.0e-92 | 175 | 411 | 238 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 5.0e-138 | 147 | 410 | 264 | + 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004601 | peroxidase activity |
| GO:0006979 | response to oxidative stress |
| GO:0020037 | heme binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEH18157.1 | 0 | 134 | 411 | 84 | 361 | cytochrome c peroxidase [Paracoccidioides brasiliensis Pb03] |
| GenBank | EEH41729.1 | 0 | 102 | 411 | 65 | 361 | cytochrome c peroxidase [Paracoccidioides brasiliensis Pb01] |
| GenBank | EEH47065.1 | 0 | 134 | 411 | 84 | 361 | cytochrome c peroxidase [Paracoccidioides brasiliensis Pb18] |
| RefSeq | XP_001697646.1 | 0 | 43 | 411 | 1 | 373 | cytochrome c peroxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002629330.1 | 0 | 58 | 412 | 29 | 364 | cytochrome c peroxidase [Ajellomyces dermatitidis SLH14081] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3riv_B | 0 | 153 | 407 | 14 | 260 | A Chain A, The Crystal Structure Of Leishmania Major Peroxidase |
| PDB | 3riv_A | 0 | 153 | 407 | 14 | 260 | A Chain A, The Crystal Structure Of Leishmania Major Peroxidase |
| PDB | 4ged_A | 0 | 153 | 407 | 13 | 259 | A Chain A, Crystal Structure Of The Leishmania Major Peroxidase-Cytochrome C Complex |
| PDB | 3riw_B | 0 | 153 | 407 | 14 | 260 | A Chain A, The Crystal Structure Of Leishmania Major Peroxidase Mutant C197t |
| PDB | 3riw_A | 0 | 153 | 407 | 14 | 260 | A Chain A, The Crystal Structure Of Leishmania Major Peroxidase Mutant C197t |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FD859200 | 269 | 145 | 413 | 0 |
| FD877284 | 261 | 153 | 413 | 0 |
| FD870404 | 257 | 157 | 413 | 0 |
| FD919958 | 250 | 164 | 413 | 0 |
| FD909260 | 245 | 169 | 413 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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