y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10024378 |
Family | AA1 |
Protein Properties | Length: 576 Molecular Weight: 62795.7 Isoelectric Point: 9.5409 |
Chromosome | Chromosome/Scaffold: 16 Start: 586298 End: 588857 |
Description | laccase 17 |
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 | 26 | 561 | 0 |
ITRHYKFNIGYTNITRLCHTRSVITVNGQLPGPRLIAREGDQVIIKVVNNVSNNITIHWHGIRQLTTGWADGPSYITQCPIQTGQSYIYNFTITGQRGTL WYHAHLSWLRSSVYGPIVILPRKNESYPFQKPYKQVPILFGEWFNVDPEAIIAQALQTGGGPNVSDAYTINGLPGPLYNCSASDTYKLKVKPGKTYLLRL INAALNDELFFGIANHSLTVVDADAVYVKPFKTEWLLLTPGQTTNVLLKTKPHSPNATFLMEAKPYFTGAGTFDNSTVAGILEYASSTTPKTKKPLPSIK PNLPSINGNISTPQVANFTAKFRSLASRRFPANVPQTVNRKFFFTVGLGTTPCPANTTCQGPTNTTKFAASINNVSFALPTVALLQSYYSGNSIGVFSSD FPQNPATPFNYTGTPPNNTNVSNGTKAVALAFNTSVEVVLQDTSILGAESHPLHLHGYNFFVVGTGFGNYNPSKDPAKFNLVDPVERNTVGVPAGGWVAI RFLADNPGVWFMHCHLDVHTSWGLRMAWVVSNGALP |
Full Sequence |
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Protein Sequence Length: 576 Download |
MGNSAMPAMI FACCILWLFP SFTAAITRHY KFNIGYTNIT RLCHTRSVIT VNGQLPGPRL 60 IAREGDQVII KVVNNVSNNI TIHWHGIRQL TTGWADGPSY ITQCPIQTGQ SYIYNFTITG 120 QRGTLWYHAH LSWLRSSVYG PIVILPRKNE SYPFQKPYKQ VPILFGEWFN VDPEAIIAQA 180 LQTGGGPNVS DAYTINGLPG PLYNCSASDT YKLKVKPGKT YLLRLINAAL NDELFFGIAN 240 HSLTVVDADA VYVKPFKTEW LLLTPGQTTN VLLKTKPHSP NATFLMEAKP YFTGAGTFDN 300 STVAGILEYA SSTTPKTKKP LPSIKPNLPS INGNISTPQV ANFTAKFRSL ASRRFPANVP 360 QTVNRKFFFT VGLGTTPCPA NTTCQGPTNT TKFAASINNV SFALPTVALL QSYYSGNSIG 420 VFSSDFPQNP ATPFNYTGTP PNNTNVSNGT KAVALAFNTS VEVVLQDTSI LGAESHPLHL 480 HGYNFFVVGT GFGNYNPSKD PAKFNLVDPV ERNTVGVPAG GWVAIRFLAD NPGVWFMHCH 540 LDVHTSWGLR MAWVVSNGAL PSQKLQPPPA DLPQC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 8.0e-47 | 38 | 557 | 562 | + 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 | 4.0e-62 | 18 | 554 | 570 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-78 | 10 | 562 | 585 | + oxidoreductase | ||
TIGR03388 | ascorbase | 1.0e-82 | 27 | 549 | 557 | + 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 | 25 | 575 | 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 | |
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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 | CAA74105.1 | 0 | 1 | 575 | 1 | 580 | laccase [Populus trichocarpa] |
RefSeq | XP_002300066.1 | 0 | 1 | 575 | 1 | 580 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002308164.1 | 0 | 1 | 575 | 1 | 580 | laccase 110b [Populus trichocarpa] |
RefSeq | XP_002329138.1 | 0 | 1 | 575 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531565.1 | 0 | 4 | 575 | 11 | 577 | 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 | 28 | 565 | 4 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asq_A | 0 | 28 | 565 | 4 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_B | 0 | 28 | 565 | 4 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_A | 0 | 28 | 565 | 4 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1aso_B | 0 | 28 | 565 | 4 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |