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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna11144.1-v1.0-hybrid |
Family | AA2 |
Protein Properties | Length: 584 Molecular Weight: 63423.3 Isoelectric Point: 7.823 |
Chromosome | Chromosome/Scaffold: 2 Start: 16492020 End: 16498082 |
Description | Peroxidase superfamily protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 51 | 309 | 0 |
HVSANPNLPAKLLRMHFHDCFVRGCDASVLLSSTANNTAERDSFPNLSLKGFDVIDDIKEQLEKACPGVVSCADILALATRDSVSFQFKKSQWDVLTGRR DGNVSIANEVSGNLPSPFFNFAQLKQSFANKGLTVQDLVVLSGAHSIGVGHCNLFSKRLYNFTGKGDQDPSMDSTYAALLKTQCQGPGDRTTTVELDPGS FQNFDNSFYTILKQKKGLFQSDAALLTNKVSSNAVQKLLKGNDFFTEFGQSMKRMGAIG |
Full Sequence |
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Protein Sequence Length: 584 Download |
MKANNISLIL LVCILVCINL GGCLGGSLRK NFYKKTCPRA EQIVKDATWN HVSANPNLPA 60 KLLRMHFHDC FVRGCDASVL LSSTANNTAE RDSFPNLSLK GFDVIDDIKE QLEKACPGVV 120 SCADILALAT RDSVSFQFKK SQWDVLTGRR DGNVSIANEV SGNLPSPFFN FAQLKQSFAN 180 KGLTVQDLVV LSGAHSIGVG HCNLFSKRLY NFTGKGDQDP SMDSTYAALL KTQCQGPGDR 240 TTTVELDPGS FQNFDNSFYT ILKQKKGLFQ SDAALLTNKV SSNAVQKLLK GNDFFTEFGQ 300 SMKRMGAIGV LTGTSGQIRT QCGFELEIDF SQYDHPVVLT VEAQAKYVGH LGGGLSKNLF 360 LKDKKSRFYI VSALADTKVD LKGGLRMAPE EALGEILQVP PGSVTPLSLV NESARHCNDY 420 EFLVLFFFDM FNPDSLHIFV FPALTTNGLD KFLKSIERDP SYVDLEANPS VGKDQPPDLA 480 SLVPSSSVVL PDPPETAASS KVPTENKVSA SNKSTKSAAS TSKPSVSATK SQDKPANITD 540 VGKLVDDLLE STSSLLLKEM IFKNTAYTEG FHAGMHCRPK RSY* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG3760 | COG3760 | 2.0e-19 | 325 | 467 | 158 | + Uncharacterized conserved protein [Function unknown] | ||
cd04335 | PrdX_deacylase | 4.0e-38 | 325 | 463 | 156 | + This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins. | ||
pfam00141 | peroxidase | 5.0e-62 | 44 | 208 | 166 | + Peroxidase. | ||
PLN03030 | PLN03030 | 5.0e-98 | 25 | 322 | 304 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 1.0e-169 | 28 | 324 | 298 | + 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 - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3hdl_A | 0 | 28 | 322 | 2 | 299 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
PDB | 1sch_B | 0 | 28 | 322 | 2 | 290 | A Chain A, Peanut Peroxidase |
PDB | 1sch_A | 0 | 28 | 322 | 2 | 290 | A Chain A, Peanut Peroxidase |
PDB | 3atj_B | 0 | 28 | 322 | 3 | 302 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 3atj_A | 0 | 28 | 322 | 3 | 302 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |