| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 106106 |
| Family | AA2 |
| Protein Properties | Length: 326 Molecular Weight: 35421.2 Isoelectric Point: 8.1034 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA2 | 55 | 308 | 0 |
| TLPPKLLRLMFHDCFIEGCDGSILVDSTANHTAEKEDESNKTVDGYAAIDSAKSALEFFCPGVVSCADIVALAAREAVIMMGGPQVQIPMGRRDGLISKV SNVRGNIPDTTLTLDQLTKVFNSKGLSQKDLIVLSGAHTVGLAHCFAFNERFHFSSNGSVKVDSTLDPGFARQLLQACPERPNPRVAVAIDPTTPNAFDN AYYRNLQNGKGLFGSDQVLFTDRRSRQAVNSLSGDSREFFGSWADSFLKLSVVH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 326 Download |
| MGTSVRHWKQ RLVLVCLALG SVCGQLAFDF YANSCPRVEA VVANAIRSAT FFDSTLPPKL 60 LRLMFHDCFI EGCDGSILVD STANHTAEKE DESNKTVDGY AAIDSAKSAL EFFCPGVVSC 120 ADIVALAARE AVIMMGGPQV QIPMGRRDGL ISKVSNVRGN IPDTTLTLDQ LTKVFNSKGL 180 SQKDLIVLSG AHTVGLAHCF AFNERFHFSS NGSVKVDSTL DPGFARQLLQ ACPERPNPRV 240 AVAIDPTTPN AFDNAYYRNL QNGKGLFGSD QVLFTDRRSR QAVNSLSGDS REFFGSWADS 300 FLKLSVVHTK TGNQGEVRRR CRAFN* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00141 | peroxidase | 0.005 | 258 | 289 | 32 | + Peroxidase. | ||
| cd00691 | ascorbate_peroxidase | 1.0e-22 | 58 | 305 | 270 | + 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-54 | 38 | 196 | 160 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 5.0e-75 | 12 | 325 | 322 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 3.0e-146 | 25 | 324 | 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. | ||
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1sch_B | 0 | 25 | 325 | 1 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 1sch_A | 0 | 25 | 325 | 1 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 3hdl_A | 0 | 26 | 325 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 1qo4_A | 0 | 25 | 325 | 2 | 304 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 1pa2_A | 0 | 25 | 325 | 2 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |
