y
Basic Information | |
---|---|
Species | Thellungiella halophila |
Cazyme ID | Thhalv10022797m |
Family | AA2 |
Protein Properties | Length: 289 Molecular Weight: 31818.1 Isoelectric Point: 6.1129 |
Chromosome | Chromosome/Scaffold: 11 Start: 2883177 End: 2886154 |
Description | ascorbate peroxidase 3 |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA2 | 20 | 244 | 0 |
ELRSLIAKKNCAPIMLRLAWHDAGTYDAKSKTGGPNGSIRNETEYSHGANSGLKIALDLCEDVKSKLPKISYADLYQLAGVVAVEVTGGPDISFVPGRKD CNDCTDEGRLPDANQGFKHLKDVFYRMGLSDKDIVALSGAHTLGRAHPERSGFDGPWTQDPLKFDNSYFVELLKEEESEGLLKLSTDKTLLEVPEFRHYV ELYAKDEDAFFRDYAESHKKLSELG |
Full Sequence |
---|
Protein Sequence Length: 289 Download |
MAALVVDAEY LKEVEKARRE LRSLIAKKNC APIMLRLAWH DAGTYDAKSK TGGPNGSIRN 60 ETEYSHGANS GLKIALDLCE DVKSKLPKIS YADLYQLAGV VAVEVTGGPD ISFVPGRKDC 120 NDCTDEGRLP DANQGFKHLK DVFYRMGLSD KDIVALSGAH TLGRAHPERS GFDGPWTQDP 180 LKFDNSYFVE LLKEEESEGL LKLSTDKTLL EVPEFRHYVE LYAKDEDAFF RDYAESHKKL 240 SELGFTPTSS IAKAITDSTV LAHSAVGVAV AAAVVAFGYF YEIRRKMK* 300 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 3.0e-49 | 17 | 225 | 219 | + Peroxidase. | ||
PLN02879 | PLN02879 | 5.0e-99 | 6 | 245 | 240 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 3.0e-99 | 6 | 245 | 241 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 2.0e-144 | 2 | 247 | 252 | + 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. | ||
PLN02608 | PLN02608 | 0 | 1 | 288 | 290 | + L-ascorbate peroxidase |
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 | AAB52954.1 | 0 | 1 | 288 | 1 | 288 | ascorbate peroxidase [Gossypium hirsutum] |
GenBank | AAL35365.1 | 0 | 1 | 288 | 1 | 287 | AF442387_1 ascorbate peroxidase [Capsicum annuum] |
GenBank | ABA10744.1 | 0 | 1 | 288 | 1 | 287 | cytosolic ascorbate peroxidase isoform 4 [Solanum lycopersicum] |
EMBL | CAA06823.1 | 0 | 1 | 288 | 1 | 287 | ascorbate peroxidase [Arabidopsis thaliana] |
RefSeq | NP_195226.1 | 0 | 1 | 288 | 1 | 287 | APX3 (ASCORBATE PEROXIDASE 3); L-ascorbate peroxidase [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2xj6_A | 0 | 5 | 245 | 6 | 246 | A Chain A, Crystal Structure Of Hedgehog-interacting Protein (hhip) |
PDB | 2xih_A | 0 | 5 | 245 | 6 | 246 | A Chain A, Crystal Structure Of Hedgehog-interacting Protein (hhip) |
PDB | 2xif_A | 0 | 5 | 245 | 6 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 5 | 245 | 6 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 0 | 5 | 245 | 18 | 258 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |