Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29703.m001530 |
Family | AA1 |
Protein Properties | Length: 510 Molecular Weight: 57202 Isoelectric Point: 4.3215 |
Chromosome | Chromosome/Scaffold: 29703 Start: 315545 End: 318355 |
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 | 4 | 470 | 0 |
LHGVKQPRNPWSDGPEYITQCGIQPGTNFTYEVIFSDEVGTLWWHAHSDWTRNTVHGAIVIHPEEGTSYPYPTPDGEEVLVLGSWYTYDVNLVVAEDLLI GGDLPASDAYTINGEPGDFCNCSKESTYRRQVEYGKTYLLRLVNAIMNTEVFFAIAGHNVTVVGRDAAYLKPFVTSYIMMGPGQTMDILLTTDQSPGQYY IAARQLYTDKSSFTDYDKVNVTAILEYKGNYSYPTSFPYDTLPSYTDIDAGVAFRNKLRSLYNQDVPKNITTWMYITAAQNLLALNQPDGGAVSTLAASL NNVSFVNPKTDVLQAYYYNISGFFTEDFPDMPPTFYDFVADDFLVNSTESVLGTKVKVLEYGEEVEMIFQNSNILNASEDHPMHLHGYSFYVVGAGPGNF DFEEDPEKYNLVDPPYVNTATLPKVGWLSVRFRALNPGVWLWHCHLDRHLSWGMDTVIIVKDGGTPE |
Full Sequence |
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Protein Sequence Length: 510 Download |
MILLHGVKQP RNPWSDGPEY ITQCGIQPGT NFTYEVIFSD EVGTLWWHAH SDWTRNTVHG 60 AIVIHPEEGT SYPYPTPDGE EVLVLGSWYT YDVNLVVAED LLIGGDLPAS DAYTINGEPG 120 DFCNCSKEST YRRQVEYGKT YLLRLVNAIM NTEVFFAIAG HNVTVVGRDA AYLKPFVTSY 180 IMMGPGQTMD ILLTTDQSPG QYYIAARQLY TDKSSFTDYD KVNVTAILEY KGNYSYPTSF 240 PYDTLPSYTD IDAGVAFRNK LRSLYNQDVP KNITTWMYIT AAQNLLALNQ PDGGAVSTLA 300 ASLNNVSFVN PKTDVLQAYY YNISGFFTED FPDMPPTFYD FVADDFLVNS TESVLGTKVK 360 VLEYGEEVEM IFQNSNILNA SEDHPMHLHG YSFYVVGAGP GNFDFEEDPE KYNLVDPPYV 420 NTATLPKVGW LSVRFRALNP GVWLWHCHLD RHLSWGMDTV IIVKDGGTPE TCIRKPPPNM 480 PICDDAPALG LSRADSSSED LQQKYENTYT |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02835 | PLN02835 | 6.0e-38 | 5 | 443 | 447 | + oxidoreductase | ||
PLN02191 | PLN02191 | 1.0e-54 | 1 | 462 | 491 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-69 | 5 | 460 | 481 | + oxidoreductase | ||
TIGR03388 | ascorbase | 6.0e-75 | 5 | 460 | 483 | + 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 | 5 | 483 | 486 | + 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 | 1 | 476 | 58 | 549 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asq_A | 0 | 1 | 476 | 58 | 549 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asp_B | 0 | 1 | 476 | 58 | 549 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1asp_A | 0 | 1 | 476 | 58 | 549 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 1aso_B | 0 | 1 | 476 | 58 | 549 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
Sequence Alignments (This image is cropped. Click for full image.) |
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