y
Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr8g062780.1 |
Family | AA2 |
Protein Properties | Length: 330 Molecular Weight: 36656.8 Isoelectric Point: 7.2166 |
Chromosome | Chromosome/Scaffold: 8 Start: 15728120 End: 15729394 |
Description | Peroxidase superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 36 | 307 | 0 |
EDIVKQTVTDKQKTTPSTAGAALRLFFSDCMIGGCDASVLVSSNSFNKAERDADINLSLSGDGFEVVTRAKNMLELECPGVVSCADILAAAARDLVVSVG GPFYELDLGRRDSLESKSIDAENKYPLPTMTNSQVIDIFTSKGFTVQEMVALAGAHTIGFSHCKQFSNRLFNFSKTTETDPKYNPEYAAGLKKLCQNYQK DTSMSAFNDVMTPSKFDNMYFKNLKRGMGLLATDSLMGEDKRTKPFVDMYAENQTKFFEDFGNAMRKLSVLH |
Full Sequence |
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Protein Sequence Length: 330 Download |
MIYKSYIFSL LCLALFPITQ SKLIPNYYQK SCPKFEDIVK QTVTDKQKTT PSTAGAALRL 60 FFSDCMIGGC DASVLVSSNS FNKAERDADI NLSLSGDGFE VVTRAKNMLE LECPGVVSCA 120 DILAAAARDL VVSVGGPFYE LDLGRRDSLE SKSIDAENKY PLPTMTNSQV IDIFTSKGFT 180 VQEMVALAGA HTIGFSHCKQ FSNRLFNFSK TTETDPKYNP EYAAGLKKLC QNYQKDTSMS 240 AFNDVMTPSK FDNMYFKNLK RGMGLLATDS LMGEDKRTKP FVDMYAENQT KFFEDFGNAM 300 RKLSVLHVKE GKDGEIRNRC DTFNNLNAN* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 9.0e-5 | 257 | 288 | 32 | + Peroxidase. | ||
cd00691 | ascorbate_peroxidase | 3.0e-27 | 117 | 310 | 205 | + 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. | ||
pfam00141 | peroxidase | 5.0e-50 | 51 | 193 | 143 | + Peroxidase. | ||
PLN03030 | PLN03030 | 2.0e-62 | 4 | 324 | 334 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 9.0e-141 | 22 | 321 | 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN74068.1 | 0 | 7 | 326 | 20 | 339 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002267024.1 | 0 | 7 | 326 | 6 | 325 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002280359.1 | 0 | 19 | 326 | 18 | 325 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002280547.1 | 0 | 19 | 324 | 18 | 323 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002312775.1 | 0 | 10 | 324 | 12 | 326 | predicted protein [Populus trichocarpa] |
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 | 0 | 27 | 325 | 6 | 304 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 1sch_B | 0 | 22 | 320 | 1 | 290 | A Chain A, Peanut Peroxidase |
PDB | 1sch_A | 0 | 22 | 320 | 1 | 290 | A Chain A, Peanut Peroxidase |
PDB | 1qo4_A | 0 | 22 | 324 | 2 | 304 | A Chain A, Peanut Peroxidase |
PDB | 1pa2_A | 0 | 22 | 324 | 2 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |