Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.H04936.1 |
Family | AA1 |
Protein Properties | Length: 594 Molecular Weight: 66905 Isoelectric Point: 4.7789 |
Chromosome | Chromosome/Scaffold: 8 Start: 70135629 End: 70140335 |
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 | 31 | 557 | 0 |
VHYHDFVLKEKNYTRLCSTKSMLVVNDSFPGPTIYVKKGDTLYVNVRNQGGYGVTIHWHGVNQPRNPWFDGAEYVTQCNISPGTNFTYQVLFTEEEGSLW WHAHSEWARYSIHGLIVIHPADGTSYPFPQPDGEKEMVLASWYTEDVYESIAEKLAAGSDLLVSEAYTINGEPGDFCECSNETTHRWMVDYGKTYLLRLL NAGMNAELFFAIADHNVTVVGSDAAYLKPFSSEYILISPGQTIDVLVTANQPPGQYYVAARQYYSNMFKYSGYDHTNATAILEYSGNYTAPSTPVFPSGL PSYTNYKAATGFVQSMRNIIDHVNVPMNITTRMFITVSLNQFMVEINDTTEEVYPSASVNNISWYNPWTDVLQAYYRNVSGFYTTDFPDDPPTFFNFTQH NLPLNTTAEPERGTKVKVLEYNEEVEIVFQNTDVMNSSENHPMHLHGHSFYVLGTGFGIYNNETDPLTFNLIDPPYQNTASVPKDGWLAIRFKASNPGVW LWHCHLDKHLTWGMNSVFIVKNGGTED |
Full Sequence |
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Protein Sequence Length: 594 Download |
MAVCATKLLV SAFVVVGLLL LLSASIVHGD VHYHDFVLKE KNYTRLCSTK SMLVVNDSFP 60 GPTIYVKKGD TLYVNVRNQG GYGVTIHWHG VNQPRNPWFD GAEYVTQCNI SPGTNFTYQV 120 LFTEEEGSLW WHAHSEWARY SIHGLIVIHP ADGTSYPFPQ PDGEKEMVLA SWYTEDVYES 180 IAEKLAAGSD LLVSEAYTIN GEPGDFCECS NETTHRWMVD YGKTYLLRLL NAGMNAELFF 240 AIADHNVTVV GSDAAYLKPF SSEYILISPG QTIDVLVTAN QPPGQYYVAA RQYYSNMFKY 300 SGYDHTNATA ILEYSGNYTA PSTPVFPSGL PSYTNYKAAT GFVQSMRNII DHVNVPMNIT 360 TRMFITVSLN QFMVEINDTT EEVYPSASVN NISWYNPWTD VLQAYYRNVS GFYTTDFPDD 420 PPTFFNFTQH NLPLNTTAEP ERGTKVKVLE YNEEVEIVFQ NTDVMNSSEN HPMHLHGHSF 480 YVLGTGFGIY NNETDPLTFN LIDPPYQNTA SVPKDGWLAI RFKASNPGVW LWHCHLDKHL 540 TWGMNSVFIV KNGGTEDTSI RDPPGYMPPC YPDSKLRLEE FSDSDEKLYS TLM* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-47 | 28 | 552 | 577 | + 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-66 | 47 | 549 | 535 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 1.0e-82 | 47 | 548 | 534 | + 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. | ||
PLN02604 | PLN02604 | 1.0e-83 | 47 | 548 | 523 | + oxidoreductase | ||
TIGR03389 | laccase | 0 | 31 | 570 | 545 | + 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 | 1 | 585 | 1 | 584 | laccase, putative [Ricinus communis] |
RefSeq | XP_002524788.1 | 0 | 8 | 585 | 8 | 586 | laccase, putative [Ricinus communis] |
RefSeq | XP_002524792.1 | 0 | 27 | 578 | 29 | 573 | laccase, putative [Ricinus communis] |
RefSeq | XP_002527100.1 | 0 | 29 | 585 | 23 | 580 | laccase, putative [Ricinus communis] |
RefSeq | XP_002530554.1 | 0 | 9 | 578 | 7 | 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 | 47 | 548 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asq_A | 0 | 47 | 548 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_B | 0 | 47 | 548 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_A | 0 | 47 | 548 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1aso_B | 0 | 47 | 548 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |