Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.L01345.1 |
Family | AA1 |
Protein Properties | Length: 528 Molecular Weight: 58677.3 Isoelectric Point: 6.5881 |
Chromosome | Chromosome/Scaffold: 186 Start: 24360 End: 26710 |
Description | laccase 14 |
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 | 2 | 516 | 0 |
LCETNRTVLTVNGLFPGPEIRAHKGDTIYVNVTNIGPYGVTIHWHGVRQIRYPWSDGPENITQCPIPTNSSFLQKVILTEEEGTLWWHAHSDWTRATVHG PIIVLPVGDTNYPYKFDEQHTIVIAEWYARDTKAIIDEALATGGDPDLSVAYTINGQPGDTYPCSNGLMYNITVMQGKTYLFRIIHSGMNEEMFFSIAKH NLTVVGMDGAYLKPLKTNYLMITPGQTMDVLVTTNQRPGHYYMLFSPFVDTNAPSNENVTRGIFQYSGSYNHSETPALPELPGFTNKSDAGNFTIQLRSL NSKEHLSTVPTKITRNITITVSVNQQPCPTNKTCLGPQGSVHSASLNNISFSTPSISILQAYYNNINGVYNKTFPDKPPFVFDYTGNVSALGEVAFVSTK VLMIKYNEEVEIRFQGTNFGAAENHPMHLHGYSFYVVGMGDGNFSDSYVSQYNTVDPPYINTVGLPKNGWTAIRFKANNPGVWFMHCHLERHASWGMDTV LIVGEGPNKDQKMLP |
Full Sequence |
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Protein Sequence Length: 528 Download |
MLCETNRTVL TVNGLFPGPE IRAHKGDTIY VNVTNIGPYG VTIHWHGVRQ IRYPWSDGPE 60 NITQCPIPTN SSFLQKVILT EEEGTLWWHA HSDWTRATVH GPIIVLPVGD TNYPYKFDEQ 120 HTIVIAEWYA RDTKAIIDEA LATGGDPDLS VAYTINGQPG DTYPCSNGLM YNITVMQGKT 180 YLFRIIHSGM NEEMFFSIAK HNLTVVGMDG AYLKPLKTNY LMITPGQTMD VLVTTNQRPG 240 HYYMLFSPFV DTNAPSNENV TRGIFQYSGS YNHSETPALP ELPGFTNKSD AGNFTIQLRS 300 LNSKEHLSTV PTKITRNITI TVSVNQQPCP TNKTCLGPQG SVHSASLNNI SFSTPSISIL 360 QAYYNNINGV YNKTFPDKPP FVFDYTGNVS ALGEVAFVST KVLMIKYNEE VEIRFQGTNF 420 GAAENHPMHL HGYSFYVVGM GDGNFSDSYV SQYNTVDPPY INTVGLPKNG WTAIRFKANN 480 PGVWFMHCHL ERHASWGMDT VLIVGEGPNK DQKMLPPPQH MPPCSGL* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
TIGR03390 | ascorbOXfungal | 3.0e-53 | 3 | 506 | 554 | + 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-57 | 9 | 505 | 538 | + L-ascorbate oxidase |
PLN02604 | PLN02604 | 3.0e-71 | 7 | 501 | 530 | + oxidoreductase |
TIGR03388 | ascorbase | 7.0e-77 | 9 | 521 | 545 | + 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 | 2 | 524 | 525 | + 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 | |
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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 | ACI46953.1 | 0 | 2 | 525 | 44 | 567 | putative lacasse/diphenol oxidase [Castanea mollissima] |
RefSeq | XP_002270959.1 | 0 | 2 | 524 | 78 | 601 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002325572.1 | 0 | 2 | 525 | 30 | 552 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002325575.1 | 0 | 2 | 525 | 30 | 552 | multicopper oxidase [Populus trichocarpa] |
RefSeq | XP_002527130.1 | 0 | 2 | 525 | 45 | 571 | laccase, 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 | 3 | 505 | 19 | 524 | 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 | 3 | 505 | 19 | 524 | 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 | 3 | 505 | 19 | 524 | 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 | 3 | 505 | 19 | 524 | 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 | 3 | 505 | 19 | 524 | A Chain A, Structural Basis For Light Acitvation Of A Chloroplast Enzyme. The Structure Of Sorghum Nadp-Malate Dehydrogenase In Its Oxidized Form |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797675 | 498 | 33 | 524 | 0 |
FY788003 | 191 | 1 | 191 | 0 |
FY788004 | 210 | 316 | 525 | 0 |
FY827568 | 222 | 192 | 413 | 0 |
EE591979 | 563 | 2 | 519 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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