Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.H04937.1 |
Family | AA1 |
Protein Properties | Length: 543 Molecular Weight: 61431.2 Isoelectric Point: 4.6567 |
Chromosome | Chromosome/Scaffold: 8 Start: 70156628 End: 70161110 |
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 | 506 | 0 |
LVVNDSFPGPTIYVKKGDTLYVNVHNQGAYGITIHWHGVNQPRNPWFDGAEYVTQCSISPGTNFTYQVLFTEEEGSLWWHAHSEWARYSIHGFIVIHPAD GTSYPFPQPDGEKEMVLASWYTEDVYASIAEKLAAGSDLLVSEAYTINGEPGDFCECSNETTHRWMVDYGKTYLLRLLNADMNAELFFAIADHNVTVVGS DAAYLKPFSSEIVFISPGQTIDVLVTANQPPGRYYIAARQYYSNQFKFSEYDHANATAILEYSGNYTAPSTPVFPSGLPSYTNYKAATGFVQSMRNIIDH VNVPINITTRMYITVSLNKFTLEINDTTEESYPSASLNNISWYNPWTDVLQAYYRNISGFYTTDFPEFPPTFFNFTQHNLPLNTTNEPERGTKVKVLEYN EEVEIVFQNTDVANSSENHPMHLHGHSFYVLGTGFGNYNNETDPLTFNLIDPPYQNTASVPKDGWLAIRFRASNPGVWLWHCHLDKHLTWGMNSVFIVKN GGTED |
Full Sequence |
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Protein Sequence Length: 543 Download |
MLVVNDSFPG PTIYVKKGDT LYVNVHNQGA YGITIHWHGV NQPRNPWFDG AEYVTQCSIS 60 PGTNFTYQVL FTEEEGSLWW HAHSEWARYS IHGFIVIHPA DGTSYPFPQP DGEKEMVLAS 120 WYTEDVYASI AEKLAAGSDL LVSEAYTING EPGDFCECSN ETTHRWMVDY GKTYLLRLLN 180 ADMNAELFFA IADHNVTVVG SDAAYLKPFS SEIVFISPGQ TIDVLVTANQ PPGRYYIAAR 240 QYYSNQFKFS EYDHANATAI LEYSGNYTAP STPVFPSGLP SYTNYKAATG FVQSMRNIID 300 HVNVPINITT RMYITVSLNK FTLEINDTTE ESYPSASLNN ISWYNPWTDV LQAYYRNISG 360 FYTTDFPEFP PTFFNFTQHN LPLNTTNEPE RGTKVKVLEY NEEVEIVFQN TDVANSSENH 420 PMHLHGHSFY VLGTGFGNYN NETDPLTFNL IDPPYQNTAS VPKDGWLAIR FRASNPGVWL 480 WHCHLDKHLT WGMNSVFIVK NGGTEDTSIR DPPSYMPSCY PDSKLRLEEF SNSDEKLYST 540 SM* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 2.0e-43 | 3 | 501 | 545 | + 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 | 4.0e-65 | 1 | 498 | 530 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-80 | 1 | 497 | 517 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-81 | 4 | 497 | 521 | + 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 | 519 | 523 | + 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 |
RefSeq | XP_002524785.1 | 0 | 2 | 534 | 52 | 584 | laccase, putative [Ricinus communis] |
RefSeq | XP_002524788.1 | 0 | 2 | 536 | 53 | 588 | laccase, putative [Ricinus communis] |
RefSeq | XP_002524792.1 | 0 | 2 | 527 | 55 | 573 | laccase, putative [Ricinus communis] |
RefSeq | XP_002527100.1 | 0 | 2 | 534 | 47 | 580 | laccase, putative [Ricinus communis] |
RefSeq | XP_002530554.1 | 0 | 2 | 527 | 47 | 569 | 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 | 1 | 497 | 24 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asq_A | 0 | 1 | 497 | 24 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_B | 0 | 1 | 497 | 24 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_A | 0 | 1 | 497 | 24 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1aso_B | 0 | 1 | 497 | 24 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
JK801464 | 269 | 27 | 295 | 0 |
CO094726 | 283 | 39 | 318 | 0 |
HO797675 | 500 | 25 | 519 | 0 |
EE591979 | 562 | 1 | 514 | 0 |
CO126470 | 252 | 1 | 252 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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