Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.I00388.1 |
Family | AA1 |
Protein Properties | Length: 572 Molecular Weight: 64304.2 Isoelectric Point: 7.5208 |
Chromosome | Chromosome/Scaffold: 9 Start: 7340582 End: 7343943 |
Description | Cupredoxin superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 301 | 548 | 2.8026e-45 |
VGRDATAKTPPGLAILNYYPNHPKRVPPTDPPAGPIWNDTAPRLAQSVAIKARQGYVHTPPPKSDRVIVLLNTQNKIDGYIRWSVNNVSFTFPHTPYLIA LKENLHHVFDQHPPPDRLHEFTTYDIYGVVNNTNATSSNAIYRLKFNSTVDIILQNANTMTENNSETHPWHLHGHDFWVLGYGKGKFDAKNDPKKYNLAN PIMKNTVAVHPYGWTALRFVADNPGVWLFHCHIESHFYMGMRVVFEEG | |||
AA1 | 75 | 347 | 0 |
NLAIHWHGIRQIGSPWSDGTEGVTQCPILPGDNFTYRFIVDRPGTYLYHAHYGMQREAGLYGSIRVLLPDGVAEPFTYDYDRSIILNDWYHASTYEQAAG LSSIPFVWVEEPQSLLIQGKGKFDCSKLVTASSDPMACNTTNPECSPYMLTVVQGKTYRLRISSVTALSALSFQIEGHNMTVVEADGHYVEPIVVQNLFI YSGETYSVLIKIDQEPSRNYWITTNIVGRDATAKTPPGLAILNYYPNHPKRVPPTDPPAGPIWNDTAPRLAQS |
Full Sequence |
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Protein Sequence Length: 572 Download |
MSRSIAWLLC VFAVMVSAEA GVRRYKWDVK YEFKSLDCYK KLAITINGKT PGPTILARQG 60 DTIIVEVTNG LVTENLAIHW HGIRQIGSPW SDGTEGVTQC PILPGDNFTY RFIVDRPGTY 120 LYHAHYGMQR EAGLYGSIRV LLPDGVAEPF TYDYDRSIIL NDWYHASTYE QAAGLSSIPF 180 VWVEEPQSLL IQGKGKFDCS KLVTASSDPM ACNTTNPECS PYMLTVVQGK TYRLRISSVT 240 ALSALSFQIE GHNMTVVEAD GHYVEPIVVQ NLFIYSGETY SVLIKIDQEP SRNYWITTNI 300 VGRDATAKTP PGLAILNYYP NHPKRVPPTD PPAGPIWNDT APRLAQSVAI KARQGYVHTP 360 PPKSDRVIVL LNTQNKIDGY IRWSVNNVSF TFPHTPYLIA LKENLHHVFD QHPPPDRLHE 420 FTTYDIYGVV NNTNATSSNA IYRLKFNSTV DIILQNANTM TENNSETHPW HLHGHDFWVL 480 GYGKGKFDAK NDPKKYNLAN PIMKNTVAVH PYGWTALRFV ADNPGVWLFH CHIESHFYMG 540 MRVVFEEGVE KVSKLPSEIM GCGETKAFKK P* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 2.0e-85 | 38 | 548 | 542 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
TIGR03389 | laccase | 5.0e-113 | 20 | 562 | 575 | + laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. | ||
PLN02604 | PLN02604 | 0 | 1 | 566 | 568 | + oxidoreductase | ||
TIGR03388 | ascorbase | 0 | 22 | 565 | 546 | + L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. | ||
PLN02191 | PLN02191 | 0 | 1 | 568 | 572 | + L-ascorbate oxidase |
Gene Ontology | |
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GO Term | Description |
GO:0005507 | copper ion binding |
GO:0016491 | oxidoreductase activity |
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 |
GenBank | AAY47050.1 | 0 | 13 | 571 | 26 | 578 | ascorbate oxidase [Solanum lycopersicum] |
DDBJ | BAB86897.1 | 0 | 18 | 571 | 21 | 567 | syringolide-induced protein B13-1-1 [Glycine max] |
RefSeq | XP_002281435.1 | 0 | 3 | 568 | 2 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306323.1 | 0 | 9 | 571 | 6 | 570 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528975.1 | 0 | 3 | 571 | 9 | 576 | l-ascorbate oxidase, putative [Ricinus communis] |
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 | 1asq_B | 0 | 22 | 565 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asq_A | 0 | 22 | 565 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asp_B | 0 | 22 | 565 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asp_A | 0 | 22 | 565 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1aso_B | 0 | 22 | 565 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |