y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 126863 |
Family | AA2 |
Protein Properties | Length: 336 Molecular Weight: 36953.5 Isoelectric Point: 8.7317 |
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 | 44 | 312 | 0 |
DTINEHASRDPTIPAGLIRLHFHDCFVNGCDGSILLDSTPTDGTNVEKFAPPNRDSARGFEVIEDAKRRLEQACPGIVSCADTVAIAARDSTVKMGGQHY IVATGRYDGRVSSLQLATNIPSPSMDASTLIENFKNQGLSVQDLVVLSGAHTLGTSKCNFFASGRFDRLYNFRNTSRGDETVNPAYLQHLRNRCPREGSA NTVELDKGSQFSFDNSYFKNLERRNGLLTSDQVLFESERTSGLVRSYAYNSRQFASHFGQSMVRMGSIG |
Full Sequence |
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Protein Sequence Length: 336 Download |
MAFPKRATVS ILVVVFLSLI SSRNVLASHS YARTCPNAES IIRDTINEHA SRDPTIPAGL 60 IRLHFHDCFV NGCDGSILLD STPTDGTNVE KFAPPNRDSA RGFEVIEDAK RRLEQACPGI 120 VSCADTVAIA ARDSTVKMGG QHYIVATGRY DGRVSSLQLA TNIPSPSMDA STLIENFKNQ 180 GLSVQDLVVL SGAHTLGTSK CNFFASGRFD RLYNFRNTSR GDETVNPAYL QHLRNRCPRE 240 GSANTVELDK GSQFSFDNSY FKNLERRNGL LTSDQVLFES ERTSGLVRSY AYNSRQFASH 300 FGQSMVRMGS IGWKTKENGE IRTVCNAVNV NKHKL* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 0.0006 | 262 | 293 | 32 | + Peroxidase. | ||
cd00314 | plant_peroxidase_like | 3.0e-28 | 40 | 310 | 304 | + 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-63 | 42 | 195 | 154 | + Peroxidase. | ||
PLN03030 | PLN03030 | 4.0e-95 | 31 | 329 | 305 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 1.0e-155 | 31 | 328 | 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. |
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 | 31 | 329 | 8 | 304 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1pa2_A | 0 | 31 | 329 | 8 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 1qgj_B | 0 | 26 | 329 | 2 | 299 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1qgj_A | 0 | 26 | 329 | 2 | 299 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1sch_B | 0 | 26 | 329 | 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 |