y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.136460.2 |
Family | AA1 |
Protein Properties | Length: 476 Molecular Weight: 52929.3 Isoelectric Point: 8.1789 |
Chromosome | Chromosome/Scaffold: 01044 Start: 1074868 End: 1078068 |
Description | Laccase/Diphenol oxidase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 2 | 461 | 0 |
HGVRQLRSGWADGPAYITQCPIQPGQNYVYNFTLSSQRGTLLWHAHFSWIRATVHGAIVIFPKHGVPYPFPHPYKQKTIILGEWWKSDVEAMVNKSTQLG QPPNVSDAQTINGHPGHVPGCATKRGFTLHVETGKTYLLRIINAALNEDFFFKIASHHFTIVEVDASYTKPFKTNTIFISPGQTTNALVRAHRPIGKYLI AASPFMDAPVAIDNLTATAFLRYKRTPKNSPIVFTHIPPPNSTLLTNQFTDSLRSLNSEEYPAKVPLFIDHNLFFTVGVGVNPCETCVNGVRLVAAVNNV TFLMPQISLLQSHYYNIPGVFTDDFPANPPFVYDYTGKPPTNNQTSNGTKVYRLRFNSTVQLVLQDTAVIAPESHPIHLHGFNVFIVGTGLGNFDPIEDW KGFNLVDPVERNTFGVPNGGWIAIRFRADNPGVWFLHCHLEVHTTWGLRMAFLVENGEGP |
Full Sequence |
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Protein Sequence Length: 476 Download |
MHGVRQLRSG WADGPAYITQ CPIQPGQNYV YNFTLSSQRG TLLWHAHFSW IRATVHGAIV 60 IFPKHGVPYP FPHPYKQKTI ILGEWWKSDV EAMVNKSTQL GQPPNVSDAQ TINGHPGHVP 120 GCATKRGFTL HVETGKTYLL RIINAALNED FFFKIASHHF TIVEVDASYT KPFKTNTIFI 180 SPGQTTNALV RAHRPIGKYL IAASPFMDAP VAIDNLTATA FLRYKRTPKN SPIVFTHIPP 240 PNSTLLTNQF TDSLRSLNSE EYPAKVPLFI DHNLFFTVGV GVNPCETCVN GVRLVAAVNN 300 VTFLMPQISL LQSHYYNIPG VFTDDFPANP PFVYDYTGKP PTNNQTSNGT KVYRLRFNST 360 VQLVLQDTAV IAPESHPIHL HGFNVFIVGT GLGNFDPIED WKGFNLVDPV ERNTFGVPNG 420 GWIAIRFRAD NPGVWFLHCH LEVHTTWGLR MAFLVENGEG PNESLPPPPS DLPQC* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00394 | Cu-oxidase | 1.0e-39 | 79 | 225 | 151 | + Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. | ||
PLN02191 | PLN02191 | 3.0e-54 | 2 | 465 | 504 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 6.0e-66 | 2 | 453 | 487 | + oxidoreductase | ||
TIGR03388 | ascorbase | 8.0e-73 | 2 | 453 | 487 | + 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 | 475 | 479 | + 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 | CBI31539.1 | 0 | 2 | 475 | 60 | 533 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002308209.1 | 0 | 2 | 475 | 75 | 550 | laccase 1d [Populus trichocarpa] |
RefSeq | XP_002316233.1 | 0 | 2 | 475 | 82 | 555 | laccase 3 [Populus trichocarpa] |
RefSeq | XP_002322961.1 | 0 | 2 | 475 | 82 | 557 | laccase 1a [Populus trichocarpa] |
RefSeq | XP_002520425.1 | 0 | 2 | 475 | 83 | 556 | 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 | 2 | 453 | 62 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 0 | 2 | 453 | 62 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 0 | 2 | 453 | 62 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797675 | 481 | 2 | 476 | 0 |
EE591979 | 509 | 2 | 471 | 0 |
EL453925 | 325 | 2 | 326 | 0 |
DY280775 | 344 | 127 | 468 | 0 |
DY294712 | 401 | 28 | 421 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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