Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29703.m001527 |
Family | AA1 |
Protein Properties | Length: 590 Molecular Weight: 66117.7 Isoelectric Point: 4.6932 |
Chromosome | Chromosome/Scaffold: 29703 Start: 300930 End: 303980 |
Description | laccase 14 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 30 | 564 | 0 |
KVHYYDFVLEDKNFTKLCSTKSALVVNGSIPGPVVYVNKGDTMFVNVHNEGGYKVTLHWHGVKQPRNPWSDGPEYITQCGIQPGTNFTYEVIFSDEVGTL WWHAHSDWTRNTVHGAIVIHPEEGTSYPYPTPDGEEVLVLGSWYTYDVNLVVAEDLLTGADLPASDAYTINGEPGDFCNCSKETTYRWQVEYGKTYLLRL VNAIMNTEVFFAIAGHNVTVVGRDAAYLKPFVTSYIMIGPGQTMDILLTTDQSPGQYYIAARQLYTDKSIYTDYDKVNVTAILEYKGNYSYPTSPSFPYD TLPSYTDIDAGVAFRNKLRSLYNQDVPKNITTRMYITASQNLIVLNQSDGGVAVTLAASLNNVSFVNPKTDVLRAYYYNISGFFTDDFPDMPPTFYDFVA DDLLVNSTESMLATKVKVLEYGEEVEMIFQNANVLNASEDHPMHLHGHSFYAVGAGPGNFDFGEDPKKYNLVDPPYVNTATLPKVGWLAVRFRALNPGVW LWHCHLDRHLTWGMDTVIIVKNGGTPETSIREPPP |
Full Sequence |
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Protein Sequence Length: 590 Download |
MGPKKMGLLL DFILVFMSFI GLLPSTVEGK VHYYDFVLED KNFTKLCSTK SALVVNGSIP 60 GPVVYVNKGD TMFVNVHNEG GYKVTLHWHG VKQPRNPWSD GPEYITQCGI QPGTNFTYEV 120 IFSDEVGTLW WHAHSDWTRN TVHGAIVIHP EEGTSYPYPT PDGEEVLVLG SWYTYDVNLV 180 VAEDLLTGAD LPASDAYTIN GEPGDFCNCS KETTYRWQVE YGKTYLLRLV NAIMNTEVFF 240 AIAGHNVTVV GRDAAYLKPF VTSYIMIGPG QTMDILLTTD QSPGQYYIAA RQLYTDKSIY 300 TDYDKVNVTA ILEYKGNYSY PTSPSFPYDT LPSYTDIDAG VAFRNKLRSL YNQDVPKNIT 360 TRMYITASQN LIVLNQSDGG VAVTLAASLN NVSFVNPKTD VLRAYYYNIS GFFTDDFPDM 420 PPTFYDFVAD DLLVNSTESM LATKVKVLEY GEEVEMIFQN ANVLNASEDH PMHLHGHSFY 480 AVGAGPGNFD FGEDPKKYNL VDPPYVNTAT LPKVGWLAVR FRALNPGVWL WHCHLDRHLT 540 WGMDTVIIVK NGGTPETSIR EPPPYMPTCD DAPALKLFKA DFPSEDMQER |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 4.0e-53 | 35 | 551 | 565 | + 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-69 | 17 | 548 | 565 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 9.0e-86 | 12 | 546 | 560 | + oxidoreductase | ||
TIGR03388 | ascorbase | 7.0e-90 | 47 | 546 | 538 | + 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 | 29 | 569 | 549 | + 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 - 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 | 30 | 546 | 2 | 520 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asq_A | 0 | 30 | 546 | 2 | 520 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asp_B | 0 | 30 | 546 | 2 | 520 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asp_A | 0 | 30 | 546 | 2 | 520 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1aso_B | 0 | 30 | 546 | 2 | 520 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |