Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.I00385.1 |
Family | AA1 |
Protein Properties | Length: 558 Molecular Weight: 62360.9 Isoelectric Point: 7.5228 |
Chromosome | Chromosome/Scaffold: 9 Start: 7275817 End: 7278953 |
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 | 335 | 533 | 8.5e-41 |
AIKARQGYVHTPPPKSDRVIVLLNTQNTIDGYYRWSMNNVSFTFPHTPYLIALKENLHHVFDQHPPPDRLDDFTTYDIYRVANNTNAISSNAIYRLKFNS TVDIILQNANTMTENNSETHPWHLHGHDFWVLGYGTGKFDAENDPKKYNLANPIMKNTVVVHPYGWTALRLVADNPGVWFFHCHIEAHLYMGMGVVFEE |
Full Sequence |
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Protein Sequence Length: 558 Download |
MVSAEAGVRR YKWDVKYEFK FPDCYRKLAI TINGKTPGPT ILARRGDPII VEVTNGLATE 60 NLAIHWHGIR QIGSPWSDGT EGVTQCPILP GDTFIYRFVV DRPGTYLYHA HYGMQREAGL 120 YGSIRVLLPG GVAEPFTYDN DKSIILNDWY HASTYEQAAG LSSIPFVWVG EPQSLLIQGK 180 GKFNCSKLAT PSSNPTACNT TNPECSPYVL IVIPGKTYRL RISSITALSA LSFQIEGHNM 240 TIVEADGHYV EPIVVQNLFI YSGETYSVLI KIDQEPSRNY WITTNIVARN ATAKTPPGLA 300 ILNYNPNHPK RVPPTDPPAG PIWSDTAPRL AQGVAIKARQ GYVHTPPPKS DRVIVLLNTQ 360 NTIDGYYRWS MNNVSFTFPH TPYLIALKEN LHHVFDQHPP PDRLDDFTTY DIYRVANNTN 420 AISSNAIYRL KFNSTVDIIL QNANTMTENN SETHPWHLHG HDFWVLGYGT GKFDAENDPK 480 KYNLANPIMK NTVVVHPYGW TALRLVADNP GVWFFHCHIE AHLYMGMGVV FEEGVEKVGK 540 LPSEIMGCGE TKAFKKP* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 5.0e-85 | 24 | 523 | 531 | + 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 | 1.0e-104 | 6 | 523 | 546 | + 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 | 3 | 552 | 550 | + oxidoreductase | ||
TIGR03388 | ascorbase | 0 | 8 | 551 | 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 | 3 | 554 | 555 | + 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 | 2 | 557 | 29 | 578 | ascorbate oxidase [Solanum lycopersicum] |
DDBJ | BAB86897.1 | 0 | 4 | 557 | 21 | 567 | syringolide-induced protein B13-1-1 [Glycine max] |
EMBL | CAN78541.1 | 0 | 2 | 554 | 1 | 547 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306323.1 | 0 | 4 | 557 | 19 | 570 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528975.1 | 0 | 4 | 557 | 29 | 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 | 8 | 551 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asq_A | 0 | 8 | 551 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asp_B | 0 | 8 | 551 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1asp_A | 0 | 8 | 551 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
PDB | 1aso_B | 0 | 8 | 551 | 3 | 541 | A Chain A, Structure Of The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EL420184 | 281 | 1 | 281 | 0 |
CK298807 | 275 | 2 | 276 | 0 |
DV705515 | 301 | 224 | 524 | 0 |
GR847295 | 277 | 43 | 319 | 0 |
DV706195 | 294 | 224 | 517 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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