| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G144648_T01 |
| Family | AA2 |
| Protein Properties | Length: 347 Molecular Weight: 36491.4 Isoelectric Point: 8.5469 |
| Chromosome | Chromosome/Scaffold: 3 Start: 41741731 End: 41743930 |
| Description | Peroxidase superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 79 | 327 | 0 |
| PALPARLLRLHFHDCFVKGCDASILLDTAQSEKTAAPNLSVGGYEVIDAIKAQLERACPGVVSCADIVALAARDAVSYQFKASLWQVETGRRDGTVSLAS NTGALPSPFAGFAGLLQSFSDRGLNLTDLVALSGAHTIGVASCSSVTPRLYQGNASSVDPLLDSAYARTLMSSCPNPSPASATVALDGGTPFRFDSGYYT RVQQRQGTLASDAALAQNAAAAQMVADLTNPIKFYAAFSMSMKKMGRVD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 347 Download |
| MRGQTQTASA GGRWRGDGAA AWCWWWVAVV LLLGHLPSCA RAGLLESNPG LAYNFYKNSC 60 PSVDSIVRSV TWAQVAANPA LPARLLRLHF HDCFVKGCDA SILLDTAQSE KTAAPNLSVG 120 GYEVIDAIKA QLERACPGVV SCADIVALAA RDAVSYQFKA SLWQVETGRR DGTVSLASNT 180 GALPSPFAGF AGLLQSFSDR GLNLTDLVAL SGAHTIGVAS CSSVTPRLYQ GNASSVDPLL 240 DSAYARTLMS SCPNPSPASA TVALDGGTPF RFDSGYYTRV QQRQGTLASD AALAQNAAAA 300 QMVADLTNPI KFYAAFSMSM KKMGRVDVLT GANGQIRKQC RQVNTS* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00692 | ligninase | 0.0001 | 97 | 217 | 121 | + Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II 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 II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
| cd00314 | plant_peroxidase_like | 8.0e-15 | 89 | 282 | 216 | + 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 | 3.0e-54 | 67 | 216 | 151 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 3.0e-74 | 50 | 344 | 302 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 2.0e-137 | 50 | 343 | 299 | + 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 | |
|---|---|
| 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 | ACG24777.1 | 0 | 1 | 346 | 1 | 346 | peroxidase 24 precursor [Zea mays] |
| RefSeq | NP_001042703.1 | 0 | 43 | 341 | 23 | 321 | Os01g0270300 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001147423.1 | 0 | 1 | 346 | 1 | 346 | LOC100281032 [Zea mays] |
| RefSeq | XP_002455434.1 | 0 | 6 | 346 | 4 | 344 | hypothetical protein SORBIDRAFT_03g010740 [Sorghum bicolor] |
| RefSeq | XP_002516845.1 | 0 | 50 | 344 | 27 | 325 | Peroxidase 27 precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1sch_B | 0 | 51 | 344 | 2 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 1sch_A | 0 | 51 | 344 | 2 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 3hdl_A | 0 | 51 | 345 | 2 | 304 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 1qo4_A | 0 | 55 | 346 | 7 | 306 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 1pa2_A | 0 | 55 | 346 | 7 | 306 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
