| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 29703.m001531 |
| Family | AA1 |
| Protein Properties | Length: 577 Molecular Weight: 64740.4 Isoelectric Point: 5.075 |
| Chromosome | Chromosome/Scaffold: 29703 Start: 323586 End: 338981 |
| 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 | 32 | 551 | 0 |
| KIHFHDFVLEDKNFTRLCSTKSALVVNGSIPGPVVYVNKNDTLYVNVYNKGGFKVTIHWHGVKQPRNPWFDGPEYITQCAIQPGTNFTYEVIFSDEEGTL WWHAHSDWTRNTVHGAIVIYPEAGSSYPFPKPDAEEVLVFGSWYTYDVNLVVEQALATGGLLPESDAYTINSQPGEFCACSKESTYRWQVDYGKTYLLRI VNANMNAQMFFAIAEHNLTIVGMDGAYLKPFVTSYIMIVPGQTMNILVTANRSLGHYYMAARKYTLQSSFSPYDKTNVTAILEYRGNYTTPASPAFPLDT LPDYDDLNAAVTFTNNLKSLHDQNVPKNITTRMYVTAATNGLLFNDTMALSASLNNVTWVNPKTDVLQAYYYNMTGFYTEDFPDMPPTFFDFVAEDLPDN TIQPLLGTKVKVLEYGEEVEMVFQTANVLNAAQNHPMHLHGHSFYVVGVGDGNFDFEEDPKTFNLVDPPSVNTATVPQSGWLAIRFKALNPGVWLWHCHF DHHLSYGMETVMIVKNGSTP | |||
| Full Sequence |
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| Protein Sequence Length: 577 Download |
| MSAVEKTGVL LEFLVAVAVA LIGFLLCKVE GKIHFHDFVL EDKNFTRLCS TKSALVVNGS 60 IPGPVVYVNK NDTLYVNVYN KGGFKVTIHW HGVKQPRNPW FDGPEYITQC AIQPGTNFTY 120 EVIFSDEEGT LWWHAHSDWT RNTVHGAIVI YPEAGSSYPF PKPDAEEVLV FGSWYTYDVN 180 LVVEQALATG GLLPESDAYT INSQPGEFCA CSKESTYRWQ VDYGKTYLLR IVNANMNAQM 240 FFAIAEHNLT IVGMDGAYLK PFVTSYIMIV PGQTMNILVT ANRSLGHYYM AARKYTLQSS 300 FSPYDKTNVT AILEYRGNYT TPASPAFPLD TLPDYDDLNA AVTFTNNLKS LHDQNVPKNI 360 TTRMYVTAAT NGLLFNDTMA LSASLNNVTW VNPKTDVLQA YYYNMTGFYT EDFPDMPPTF 420 FDFVAEDLPD NTIQPLLGTK VKVLEYGEEV EMVFQTANVL NAAQNHPMHL HGHSFYVVGV 480 GDGNFDFEED PKTFNLVDPP SVNTATVPQS GWLAIRFKAL NPGVWLWHCH FDHHLSYGME 540 TVMIVKNGST PETSIREPPV YMPPCDDAPL IRLFKSK |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03390 | ascorbOXfungal | 2.0e-50 | 37 | 547 | 551 | + 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 | 5.0e-62 | 49 | 544 | 525 | + L-ascorbate oxidase | ||
| PLN02604 | PLN02604 | 8.0e-71 | 49 | 556 | 537 | + oxidoreductase | ||
| TIGR03388 | ascorbase | 8.0e-79 | 49 | 542 | 523 | + 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 | 31 | 565 | 552 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 49 | 555 | 19 | 536 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 1asq_A | 0 | 49 | 555 | 19 | 536 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 1asp_B | 0 | 49 | 555 | 19 | 536 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 1asp_A | 0 | 49 | 555 | 19 | 536 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 1aso_B | 0 | 49 | 555 | 19 | 536 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
