Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 430498 |
Family | AA2 |
Protein Properties | Length: 595 Molecular Weight: 64135.1 Isoelectric Point: 6.9318 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 314 | 572 | 0 |
AVEKDSRTAANILRLQFHDCFVLGCDASILLDDTHTFKGEKTANPNRNSARGFEVIDEIKAALEKECEGVVSCADVLAIAARDSVVLTGGPSWEVHLGRR DSLTASRSLANRDIPPPNSTLPQLIAAFAKKGLSIVDLVALTGSHTIGVSRCASFRQRLYNFAGTRRPDPSIDPALLRSLEHICPPKGNAQETTPLDIVT PTKFDNHFFVDLELHKGVLTSDQVLFAPYAPTSALVTAFAYDQAKFFQEFVASMVRMAA |
Full Sequence |
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Protein Sequence Length: 595 Download |
MAMDRLLVPL RILFLVLAWA VDGQAEQGGF AGFPGFIPPQ LGAGFFPGAG GAQEFPPLIP 60 EITIPIPKIP EIPSIPQIPR IPEIPIVPKV PPKEVPVVPE VPKVPEVPVI PEVPKVPEVP 120 KVPAVPIIPK VPEVPPEIPT VPEIPPKVPE VPKVPEVPVP KVPEYPVVPE IPSKQPVPEV 180 PKVPEYPVVP EIPPKQPVPE VPKVPEYPVV PEIPPKQPVP EVPKVPEYPV VPKEQVPKFP 240 AIPGLLPGGM IPRPGVGGFP FPAGRGFPFP GGRPFPFPGG ATSAEMGVAV LRPGFYKEKC 300 PAAESIVKKV LQQAVEKDSR TAANILRLQF HDCFVLGCDA SILLDDTHTF KGEKTANPNR 360 NSARGFEVID EIKAALEKEC EGVVSCADVL AIAARDSVVL TGGPSWEVHL GRRDSLTASR 420 SLANRDIPPP NSTLPQLIAA FAKKGLSIVD LVALTGSHTI GVSRCASFRQ RLYNFAGTRR 480 PDPSIDPALL RSLEHICPPK GNAQETTPLD IVTPTKFDNH FFVDLELHKG VLTSDQVLFA 540 PYAPTSALVT AFAYDQAKFF QEFVASMVRM AAIKPLLGSE GQIRKECRFV NHKY* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 2.0e-10 | 325 | 570 | 268 | + 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 | 2.0e-27 | 305 | 570 | 295 | + 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 | 5.0e-61 | 307 | 460 | 154 | + Peroxidase. | ||
PLN03030 | PLN03030 | 6.0e-84 | 292 | 591 | 305 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 1.0e-164 | 291 | 590 | 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABI37011.1 | 0 | 291 | 594 | 31 | 334 | peroxidase [Oryza sativa] |
GenBank | EAY73397.1 | 0 | 291 | 594 | 35 | 338 | hypothetical protein OsI_01277 [Oryza sativa Indica Group] |
RefSeq | NP_001042657.1 | 0 | 291 | 594 | 31 | 334 | Os01g0263300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001148509.1 | 0 | 291 | 594 | 30 | 333 | peroxidase 72 [Zea mays] |
RefSeq | XP_002455406.1 | 0 | 291 | 594 | 31 | 334 | hypothetical protein SORBIDRAFT_03g010250 [Sorghum bicolor] |
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 | 1qo4_A | 0 | 291 | 591 | 3 | 304 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 1pa2_A | 0 | 291 | 591 | 3 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 4a5g_B | 0 | 291 | 591 | 4 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 4a5g_A | 0 | 291 | 591 | 4 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 1sch_B | 0 | 291 | 591 | 2 | 294 | A Chain A, Peanut Peroxidase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |