Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_96.55 |
Family | AA1 |
Protein Properties | Length: 546 Molecular Weight: 60846.8 Isoelectric Point: 9.1101 |
Chromosome | Chromosome/Scaffold: 96 Start: 850278 End: 852401 |
Description | laccase 6 |
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 | 11 | 528 | 0 |
TRFFDFKVQTLRVTKLCNTKEIVTINKRFPGPVIYAQEGDRIIVNLTNETPYNATIHWHGVRQRRSCWFDGPAYITQCPIQSGQTFRYEFTLAKQKGTLF WHAHVSWLRATVYGAIVVYPKTGVPYPFKRPDEEHIIILGEYWLKDIVQLEREVMESGGIPPPADAFTINGHPGPNYNCSANDVFEIQVVPTKTYLLRLI NAALNMENFFAIANHKLTIVETDGEYTKPFVTERVMLGPGQTMNVLVTADQPIGRYSMAMGPYMSAKHVRFQNISAIAYFQYLGAVPHTETLPAKLPSFN DNLAVMTVMDGLRSLNPVKVPKTMDVNLFVTIGVNVNKCASNNCTGLKNGTMAASMNNISFVNPSLSLLEAYYHKIDGYFTEDFPGAPLKFYDFVNGAPN NIPNDTQAMNGTRAKVLKYGSRVQLILQDTGTVTTENHPIHLHGYSFYVVGYGTGNYNPQTAKFNLVDPPYMNTIGVPVGGWAAVRFVADNPGVWFIHCH FDIHQSWGLGTVLIVKNG |
Full Sequence |
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Protein Sequence Length: 546 Download |
MGAGRAGNGS TRFFDFKVQT LRVTKLCNTK EIVTINKRFP GPVIYAQEGD RIIVNLTNET 60 PYNATIHWHG VRQRRSCWFD GPAYITQCPI QSGQTFRYEF TLAKQKGTLF WHAHVSWLRA 120 TVYGAIVVYP KTGVPYPFKR PDEEHIIILG EYWLKDIVQL EREVMESGGI PPPADAFTIN 180 GHPGPNYNCS ANDVFEIQVV PTKTYLLRLI NAALNMENFF AIANHKLTIV ETDGEYTKPF 240 VTERVMLGPG QTMNVLVTAD QPIGRYSMAM GPYMSAKHVR FQNISAIAYF QYLGAVPHTE 300 TLPAKLPSFN DNLAVMTVMD GLRSLNPVKV PKTMDVNLFV TIGVNVNKCA SNNCTGLKNG 360 TMAASMNNIS FVNPSLSLLE AYYHKIDGYF TEDFPGAPLK FYDFVNGAPN NIPNDTQAMN 420 GTRAKVLKYG SRVQLILQDT GTVTTENHPI HLHGYSFYVV GYGTGNYNPQ TAKFNLVDPP 480 YMNTIGVPVG GWAAVRFVAD NPGVWFIHCH FDIHQSWGLG TVLIVKNGKG KRERLQRPPA 540 NMPRC* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
TIGR03388 | ascorbase | 0.003 | 496 | 536 | 41 | + 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. |
PLN02191 | PLN02191 | 3.0e-68 | 27 | 524 | 541 | + L-ascorbate oxidase |
PLN02604 | PLN02604 | 3.0e-80 | 27 | 522 | 541 | + oxidoreductase |
TIGR03388 | ascorbase | 2.0e-90 | 11 | 522 | 560 | + 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 | 9 | 545 | 543 | + 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 | 7 | 545 | 29 | 571 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_182180.1 | 0 | 1 | 545 | 22 | 569 | LAC6 (laccase 6); laccase [Arabidopsis thaliana] |
RefSeq | XP_002264410.1 | 0 | 7 | 545 | 29 | 571 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002320207.1 | 0 | 21 | 545 | 1 | 529 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523314.1 | 0 | 10 | 545 | 33 | 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 | 12 | 523 | 4 | 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 | 12 | 523 | 4 | 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 | 12 | 523 | 4 | 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 |
EE591979 | 587 | 6 | 544 | 0 |
HO797675 | 502 | 53 | 546 | 0 |
EL350827 | 280 | 28 | 307 | 0 |
DW134242 | 269 | 9 | 277 | 0 |
DW157222 | 253 | 9 | 261 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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