Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.008G228500.1 |
Family | AA2 |
Protein Properties | Length: 334 Molecular Weight: 37488.1 Isoelectric Point: 5.4811 |
Chromosome | Chromosome/Scaffold: 08 Start: 51467021 End: 51468716 |
Description | Peroxidase superfamily protein |
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 | 52 | 314 | 0 |
AVLKDPRMAASLLRLHFHDCFVMGCDASILLDNHGDIISEKQAGPNLNSVRGFKVIDEIKYILEEACPLTVSCADILAMVARDAVALRGGPRWKVWLGRR DSMKASLDGANQFIPAPNSSLETLISNFNEQGLDIEDLVALSGGHTLGKARCVSFRQRVYDINMEEKRDKYKRYRTFRRILRSICPDSGRDDAIAPLDFS TPAKFDNHYYINILEGNGLLGSDNVLVTEDHEGEIIKLVWVFAANEELFFSSFAKSIVKMGNI |
Full Sequence |
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Protein Sequence Length: 334 Download |
MEIIRASFTL VVFVLNMVRI TLSVENEVLY LDYYKETCPL AEEIVSRNVE IAVLKDPRMA 60 ASLLRLHFHD CFVMGCDASI LLDNHGDIIS EKQAGPNLNS VRGFKVIDEI KYILEEACPL 120 TVSCADILAM VARDAVALRG GPRWKVWLGR RDSMKASLDG ANQFIPAPNS SLETLISNFN 180 EQGLDIEDLV ALSGGHTLGK ARCVSFRQRV YDINMEEKRD KYKRYRTFRR ILRSICPDSG 240 RDDAIAPLDF STPAKFDNHY YINILEGNGL LGSDNVLVTE DHEGEIIKLV WVFAANEELF 300 FSSFAKSIVK MGNINVLTGL EGEIRKNCRF VNP* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 1.0e-28 | 55 | 313 | 291 | + 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-65 | 45 | 197 | 153 | + Peroxidase. | ||
PLN03030 | PLN03030 | 1.0e-77 | 6 | 332 | 328 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 2.0e-157 | 29 | 331 | 305 | + 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 |
RefSeq | NP_001031486.1 | 0 | 88 | 332 | 1 | 247 | peroxidase 20 (PER20) (P20) [Arabidopsis thaliana] |
RefSeq | NP_181081.1 | 0 | 1 | 332 | 1 | 335 | peroxidase 20 (PER20) (P20) [Arabidopsis thaliana] |
RefSeq | XP_002279208.1 | 0 | 1 | 333 | 1 | 332 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002310274.1 | 0 | 29 | 332 | 32 | 332 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002326506.1 | 0 | 25 | 332 | 19 | 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 | 1qo4_A | 0 | 29 | 332 | 3 | 304 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1pa2_A | 0 | 29 | 332 | 3 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 4a5g_B | 0 | 29 | 332 | 4 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 4a5g_A | 0 | 29 | 332 | 4 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 1sch_B | 0 | 29 | 332 | 2 | 294 | A Chain A, Peanut Peroxidase |