| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.L01343.1 |
| Family | AA1 |
| Protein Properties | Length: 561 Molecular Weight: 61883.4 Isoelectric Point: 4.7253 |
| Chromosome | Chromosome/Scaffold: 186 Start: 3472 End: 6537 |
| Description | laccase 14 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA1 | 22 | 551 | 0 |
| VLYYDFVVKETPIQMLCGTNQTVLTVNGLFPGPEIHAHKGDTIYVNVTNTGPYGVTIHWHGVRQIRYPWSDGPEYITQCPIPTNSSFLQKIILTEEEGTL WWHAHSDWTRATIHGPIIILPVNGTNYPYKFDEQHTIVISEWYARDTKDIIDEALATGGDPDLSVAYTINGQPGDSYSCSNDSTYNLTAVQGKTYLLRII HSGLNEEMFFGIADHNITVVGMDGAYLKPLNTKYLMITPGQTMDVLVTANQTPGRYYMVFSPFVDTNAPSNDNVTRGIFQYTGTYNQSETPVLPELPGLT NKSDAGNFTIQLRSLNSAEHPSTVPTNITRNITITVSVNQQPCPANQTCNGPDGSMHSASLNNISFSAPSISILQAYYNNLQGVYNKTFPDTPPFVFDYT GNVSALGEAANVTTEVLMINHNEEVEIRFQGTNLGAAENHPMHLHGYSFYVVGMGDGNFSDSYVSQYNTVDPPFVNTVGLPKNGWTAIRFKADNPGVWFM HCHLERHASWGMDTVIVVKDGPNDDQKVLP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 561 Download |
| MGTFLGFVVT MTLLFCMAQG EVLYYDFVVK ETPIQMLCGT NQTVLTVNGL FPGPEIHAHK 60 GDTIYVNVTN TGPYGVTIHW HGVRQIRYPW SDGPEYITQC PIPTNSSFLQ KIILTEEEGT 120 LWWHAHSDWT RATIHGPIII LPVNGTNYPY KFDEQHTIVI SEWYARDTKD IIDEALATGG 180 DPDLSVAYTI NGQPGDSYSC SNDSTYNLTA VQGKTYLLRI IHSGLNEEMF FGIADHNITV 240 VGMDGAYLKP LNTKYLMITP GQTMDVLVTA NQTPGRYYMV FSPFVDTNAP SNDNVTRGIF 300 QYTGTYNQSE TPVLPELPGL TNKSDAGNFT IQLRSLNSAE HPSTVPTNIT RNITITVSVN 360 QQPCPANQTC NGPDGSMHSA SLNNISFSAP SISILQAYYN NLQGVYNKTF PDTPPFVFDY 420 TGNVSALGEA ANVTTEVLMI NHNEEVEIRF QGTNLGAAEN HPMHLHGYSF YVVGMGDGNF 480 SDSYVSQYNT VDPPFVNTVG LPKNGWTAIR FKADNPGVWF MHCHLERHAS WGMDTVIVVK 540 DGPNDDQKVL PPPDDVPPCS * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03390 | ascorbOXfungal | 3.0e-52 | 38 | 541 | 551 | + 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. | ||
| PLN02191 | PLN02191 | 1.0e-58 | 44 | 559 | 554 | + L-ascorbate oxidase | ||
| PLN02604 | PLN02604 | 6.0e-79 | 7 | 536 | 571 | + oxidoreductase | ||
| TIGR03388 | ascorbase | 1.0e-79 | 44 | 536 | 529 | + 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. | ||
| TIGR03389 | laccase | 0 | 20 | 559 | 542 | + 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| 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 | AAB09228.1 | 0 | 1 | 559 | 4 | 562 | laccase [Acer pseudoplatanus] |
| GenBank | ACI46953.1 | 0 | 4 | 560 | 12 | 567 | putative lacasse/diphenol oxidase [Castanea mollissima] |
| RefSeq | XP_002325572.1 | 0 | 15 | 560 | 8 | 552 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002325575.1 | 0 | 15 | 560 | 8 | 552 | multicopper oxidase [Populus trichocarpa] |
| RefSeq | XP_002527130.1 | 0 | 4 | 560 | 11 | 571 | laccase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 21 | 538 | 2 | 522 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
| PDB | 1asq_A | 0 | 21 | 538 | 2 | 522 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
| PDB | 1asp_B | 0 | 21 | 538 | 2 | 522 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
| PDB | 1asp_A | 0 | 21 | 538 | 2 | 522 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
| PDB | 1aso_B | 0 | 21 | 538 | 2 | 522 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
