y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10017426 |
Family | AA1 |
Protein Properties | Length: 487 Molecular Weight: 53481.6 Isoelectric Point: 7.7821 |
Chromosome | Chromosome/Scaffold: 511 Start: 565179 End: 567375 |
Description | laccase 5 |
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 | 1 | 472 | 0 |
MRTGWADGPEFVTQCPIRPGGSYTYRFTVRGQEGTLWWHAHSSWLRATVYGALLIQPRNGTEFPFPKPARQSTLMLGEWWNANPVDVQRESIRTGGAPNI SDAYTINGQPGDLYNCSSQDTTVVPIAAGETNLLRVINAAMNQPLFFSIANHKFTVFGADASYVKPFTTSVLMLGPGQTTDVLIVGDQPPNRYYIAARAY QSAQNAPFDNTTTTAILQYKSAPCSGGSKSCPANSKPIMPQLPAFNDTQTVTKFSTSFRSREKALVPAEIDENMLITVGLGLNPCPPNFNARQRCQAPNG TRFTASMNNVSFVLPSNFSLLQAHKQGIQGVFTSDFPAVPPRVFDYTGNVSRALWRPQNGTRLYRLKYGDRVQIVLQDTSIVTPENHPIHLHGYDFYIVA EGFGNFNPKTDTSKFNLVDPPLRNTAAVPVNGWAVIRFVADNPGVWLMHCHLDVHIGWGLATAFLVEDGVGK |
Full Sequence |
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Protein Sequence Length: 487 Download |
MRTGWADGPE FVTQCPIRPG GSYTYRFTVR GQEGTLWWHA HSSWLRATVY GALLIQPRNG 60 TEFPFPKPAR QSTLMLGEWW NANPVDVQRE SIRTGGAPNI SDAYTINGQP GDLYNCSSQD 120 TTVVPIAAGE TNLLRVINAA MNQPLFFSIA NHKFTVFGAD ASYVKPFTTS VLMLGPGQTT 180 DVLIVGDQPP NRYYIAARAY QSAQNAPFDN TTTTAILQYK SAPCSGGSKS CPANSKPIMP 240 QLPAFNDTQT VTKFSTSFRS REKALVPAEI DENMLITVGL GLNPCPPNFN ARQRCQAPNG 300 TRFTASMNNV SFVLPSNFSL LQAHKQGIQG VFTSDFPAVP PRVFDYTGNV SRALWRPQNG 360 TRLYRLKYGD RVQIVLQDTS IVTPENHPIH LHGYDFYIVA EGFGNFNPKT DTSKFNLVDP 420 PLRNTAAVPV NGWAVIRFVA DNPGVWLMHC HLDVHIGWGL ATAFLVEDGV GKLEAIEPPP 480 EDLPIC* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07731 | Cu-oxidase_2 | 1.0e-44 | 335 | 470 | 141 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 1.0e-50 | 3 | 483 | 510 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 3.0e-63 | 3 | 473 | 502 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-70 | 3 | 483 | 510 | + 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 | 2 | 486 | 489 | + 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 |
RefSeq | XP_002312187.1 | 0 | 1 | 486 | 79 | 562 | laccase 90b [Populus trichocarpa] |
RefSeq | XP_002315130.1 | 0 | 1 | 486 | 99 | 582 | laccase 90d [Populus trichocarpa] |
RefSeq | XP_002315131.1 | 0 | 1 | 486 | 96 | 575 | laccase 90c [Populus trichocarpa] |
RefSeq | XP_002520796.1 | 0 | 1 | 486 | 97 | 577 | laccase, putative [Ricinus communis] |
RefSeq | XP_002520797.1 | 0 | 1 | 486 | 99 | 581 | 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 | 3 | 476 | 69 | 531 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asq_A | 0 | 3 | 476 | 69 | 531 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asp_B | 0 | 3 | 476 | 69 | 531 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asp_A | 0 | 3 | 476 | 69 | 531 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1aso_B | 0 | 3 | 476 | 69 | 531 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY297248 | 332 | 121 | 452 | 0 |
HO797675 | 493 | 1 | 487 | 0 |
DW243722 | 285 | 163 | 447 | 0 |
FC900507 | 294 | 121 | 414 | 0 |
EX274037 | 314 | 155 | 468 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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