y
Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g016876m |
Family | AA1 |
Protein Properties | Length: 382 Molecular Weight: 41845.9 Isoelectric Point: 9.5139 |
Chromosome | Chromosome/Scaffold: 00026 Start: 1072240 End: 1074774 |
Description | laccase 3 |
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 | 13 | 364 | 0 |
TMNCNAETVRFPVEAGETILLRIINSAMNQEHFFGVANHKLTVVGVDTSYTKPFPTSVIMIAPGQTTNVLLTADQPPARYYMAAHAYNTANAAFDNTTTT AILEYKSAPFNGKKGKSRSSAPIFPILPGFNDTATATAFTARIKSLHQVQVPTVIDENLFFTVGLGLINCSNPNSPRCQGPNGTRFAASINNISFVFPRR NSLMQAYIQGQPGIFTTDFPPVPPIIFDYTGNVSRGLWQPRKRTKLYKLKFGSRVQIVFQDTSIVSVEDHPMHLHGHEFYVVGSGLGNFNPSTDTAKFNL IDPPRRNTIGTPPGGWVAVRFVAENPGIWLLHCHIDSHLTWGLAMAFLVENG |
Full Sequence |
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Protein Sequence Length: 382 Download |
MRFPSNAKVS DVTMNCNAET VRFPVEAGET ILLRIINSAM NQEHFFGVAN HKLTVVGVDT 60 SYTKPFPTSV IMIAPGQTTN VLLTADQPPA RYYMAAHAYN TANAAFDNTT TTAILEYKSA 120 PFNGKKGKSR SSAPIFPILP GFNDTATATA FTARIKSLHQ VQVPTVIDEN LFFTVGLGLI 180 NCSNPNSPRC QGPNGTRFAA SINNISFVFP RRNSLMQAYI QGQPGIFTTD FPPVPPIIFD 240 YTGNVSRGLW QPRKRTKLYK LKFGSRVQIV FQDTSIVSVE DHPMHLHGHE FYVVGSGLGN 300 FNPSTDTAKF NLIDPPRRNT IGTPPGGWVA VRFVAENPGI WLLHCHIDSH LTWGLAMAFL 360 VENGVGKLQT VQPPPLDLPR C* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 5.0e-36 | 16 | 359 | 357 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-40 | 9 | 368 | 370 | + oxidoreductase | ||
pfam07731 | Cu-oxidase_2 | 3.0e-44 | 230 | 365 | 141 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
TIGR03388 | ascorbase | 3.0e-48 | 4 | 368 | 377 | + 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 | 5.0e-155 | 15 | 381 | 373 | + 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 | NP_180580.1 | 0 | 6 | 381 | 196 | 570 | LAC3 (laccase 3); laccase [Arabidopsis thaliana] |
RefSeq | NP_196330.3 | 0 | 3 | 381 | 191 | 569 | LAC13 (laccase 13); laccase [Arabidopsis thaliana] |
RefSeq | XP_002319955.1 | 0 | 6 | 381 | 203 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002326089.1 | 0 | 6 | 381 | 203 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002516345.1 | 0 | 6 | 381 | 203 | 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 | 3e-36 | 2 | 371 | 185 | 531 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 3e-36 | 2 | 371 | 185 | 531 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 3e-36 | 2 | 371 | 185 | 531 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_A | 3e-36 | 2 | 371 | 185 | 531 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1aso_B | 3e-36 | 2 | 371 | 185 | 531 | 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 |
DY297248 | 344 | 20 | 360 | 0 |
EG529118 | 203 | 180 | 382 | 0 |
EG529116 | 203 | 180 | 382 | 0 |
EX274037 | 312 | 54 | 363 | 0 |
EY164441 | 221 | 163 | 382 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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