y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10030235 |
Family | AA1 |
Protein Properties | Length: 574 Molecular Weight: 63610.6 Isoelectric Point: 7.9743 |
Chromosome | Chromosome/Scaffold: 217 Start: 349297 End: 352935 |
Description | laccase 6 |
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 | 32 | 560 | 0 |
TTRFYDFKIQTMRVNKLCSSNEIVTVNNMFPGPVVYAEEGDRLIVKVANLSPYNTTIHWHGVRQILSCWSDGPSYITQCPITPGQSFTYEFTMVKQKGTF FWHAHVSWLRATVYGALIVYPKPGVPYPFPFPYEEHIIILGEYWNQDIVQLERRVVASGGGAPPADAYTINGHPGPNYNCSANDVYKLDVVPGRTYLLRL INAGLNTENFFAIANHKLTIVEADAEYTKPFTTDRVMLGPGQTLIVLVKADQPIGKYSMAVGPYISAQNLPFQNITSVAYFQYSGATPNSLSLPARQLPN ANDNFAVKTVMDGLKGLNTTDFVPKEIDTTLFVTIGLNINKCRSKTPQTNCQGYRNGIMAASMNNISFVKPTVSLLEAYYKGIEDYFTHDFPAAPLKFYD FVNGAPNNPPNDTSSMNGTRTKVIEYGARVQMILQDTGTISTENHPIHLHGYSFYVVGYGSGNYNPQTANLNLFDPPYMNTIGVPVGGWAAIRFKADNPG VWFIHCHFDVHQSWGLATALIVKNGVGHL |
Full Sequence |
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Protein Sequence Length: 574 Download |
MLLKLAVCAL LWLTIVISSA YSATRQWPRG STTRFYDFKI QTMRVNKLCS SNEIVTVNNM 60 FPGPVVYAEE GDRLIVKVAN LSPYNTTIHW HGVRQILSCW SDGPSYITQC PITPGQSFTY 120 EFTMVKQKGT FFWHAHVSWL RATVYGALIV YPKPGVPYPF PFPYEEHIII LGEYWNQDIV 180 QLERRVVASG GGAPPADAYT INGHPGPNYN CSANDVYKLD VVPGRTYLLR LINAGLNTEN 240 FFAIANHKLT IVEADAEYTK PFTTDRVMLG PGQTLIVLVK ADQPIGKYSM AVGPYISAQN 300 LPFQNITSVA YFQYSGATPN SLSLPARQLP NANDNFAVKT VMDGLKGLNT TDFVPKEIDT 360 TLFVTIGLNI NKCRSKTPQT NCQGYRNGIM AASMNNISFV KPTVSLLEAY YKGIEDYFTH 420 DFPAAPLKFY DFVNGAPNNP PNDTSSMNGT RTKVIEYGAR VQMILQDTGT ISTENHPIHL 480 HGYSFYVVGY GSGNYNPQTA NLNLFDPPYM NTIGVPVGGW AAIRFKADNP GVWFIHCHFD 540 VHQSWGLATA LIVKNGVGHL ETLPHPPADL PRC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 2.0e-44 | 39 | 149 | 113 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 1.0e-58 | 49 | 564 | 550 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 3.0e-60 | 49 | 564 | 553 | + oxidoreductase | ||
TIGR03388 | ascorbase | 3.0e-70 | 33 | 564 | 573 | + 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 | 33 | 573 | 546 | + 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 |
EMBL | CAN75876.1 | 0 | 5 | 573 | 1 | 571 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_182180.1 | 0 | 30 | 573 | 28 | 569 | LAC6 (laccase 6); laccase [Arabidopsis thaliana] |
RefSeq | XP_002264410.1 | 0 | 5 | 573 | 1 | 571 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002320207.1 | 0 | 43 | 573 | 1 | 529 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523314.1 | 0 | 27 | 573 | 28 | 572 | 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 | 31 | 564 | 1 | 532 | A Chain A, Crystal Structures Of Soybean Beta-Amylase Reacted With Beta-Maltose And Maltal: Active Site Components And Their Apparent Role In Catalysis |
PDB | 1asq_A | 0 | 31 | 564 | 1 | 532 | A Chain A, Crystal Structures Of Soybean Beta-Amylase Reacted With Beta-Maltose And Maltal: Active Site Components And Their Apparent Role In Catalysis |
PDB | 1asp_B | 0 | 31 | 564 | 1 | 532 | A Chain A, Crystal Structures Of Soybean Beta-Amylase Reacted With Beta-Maltose And Maltal: Active Site Components And Their Apparent Role In Catalysis |
PDB | 1asp_A | 0 | 31 | 564 | 1 | 532 | A Chain A, Crystal Structures Of Soybean Beta-Amylase Reacted With Beta-Maltose And Maltal: Active Site Components And Their Apparent Role In Catalysis |
PDB | 1aso_B | 0 | 31 | 564 | 1 | 532 | A Chain A, Crystal Structures Of Soybean Beta-Amylase Reacted With Beta-Maltose And Maltal: Active Site Components And Their Apparent Role In Catalysis |