Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.006G065800.1 |
Family | AA1 |
Protein Properties | Length: 557 Molecular Weight: 61202.7 Isoelectric Point: 9.6182 |
Chromosome | Chromosome/Scaffold: 06 Start: 18425139 End: 18428959 |
Description | Laccase/Diphenol oxidase family protein |
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 | 23 | 542 | 0 |
AMVRHYKFNVVLKNATRLCSTKPIVTVNGKFPGPTIYAREDDTVLIKVVNHVKYNVSIHWHGVRQVRTGWADGPAYITQCPIQPGQAYVYNFTLTGQRGT LWWHAHILWLRATLHGALVILPKLGVPYPFPKPNMEQVIILSEWWKSDTEAVINEALKSGLAPNVSDAHTINGHPGPVQGCASQEGFKLDVQPGNTYLLR IINAALNEELFFKIAGHELTVVEVDAVYTKPFKTDTIVITPGQTTNVLLTAKHAAGKYLVAASPFMDAPIAVDNKTATATLHYSGTLSSSLTTLTSLPPK NSTILATSFTDSLRSLNSKKYPARVPLKIDRNLLFTVSLGINPCATCVNNSRVVADINNVTFVMPKISLLQAHFFKIKGVFTDDFPGNPPVFYNFTGTQP SNLNTVNGTRLYRLAYNSTVQLVLQDTGMLTPENHPIHLHGFNFFVVGRGQGNFNPTKDPKKFNLVDPVERNTVGVPAGGWTAIRFRADNPGVWFMHCHL EIHTTWGLKMAFVVDNGKGP |
Full Sequence |
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Protein Sequence Length: 557 Download |
MAAFGIRIVL LLAAFLLPLS VEAMVRHYKF NVVLKNATRL CSTKPIVTVN GKFPGPTIYA 60 REDDTVLIKV VNHVKYNVSI HWHGVRQVRT GWADGPAYIT QCPIQPGQAY VYNFTLTGQR 120 GTLWWHAHIL WLRATLHGAL VILPKLGVPY PFPKPNMEQV IILSEWWKSD TEAVINEALK 180 SGLAPNVSDA HTINGHPGPV QGCASQEGFK LDVQPGNTYL LRIINAALNE ELFFKIAGHE 240 LTVVEVDAVY TKPFKTDTIV ITPGQTTNVL LTAKHAAGKY LVAASPFMDA PIAVDNKTAT 300 ATLHYSGTLS SSLTTLTSLP PKNSTILATS FTDSLRSLNS KKYPARVPLK IDRNLLFTVS 360 LGINPCATCV NNSRVVADIN NVTFVMPKIS LLQAHFFKIK GVFTDDFPGN PPVFYNFTGT 420 QPSNLNTVNG TRLYRLAYNS TVQLVLQDTG MLTPENHPIH LHGFNFFVVG RGQGNFNPTK 480 DPKKFNLVDP VERNTVGVPA GGWTAIRFRA DNPGVWFMHC HLEIHTTWGL KMAFVVDNGK 540 GPNESLLPPP SDLPKC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 5.0e-73 | 20 | 546 | 566 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-88 | 20 | 534 | 542 | + oxidoreductase | ||
TIGR03388 | ascorbase | 3.0e-97 | 25 | 534 | 541 | + 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 | 23 | 556 | 539 | + 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 |
GenBank | AAC49536.1 | 0 | 6 | 556 | 5 | 557 | diphenol oxidase [Nicotiana tabacum] |
RefSeq | XP_002280416.1 | 0 | 9 | 556 | 7 | 554 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299828.1 | 0 | 9 | 556 | 7 | 554 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002314124.1 | 0 | 9 | 556 | 9 | 556 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520425.1 | 0 | 9 | 556 | 9 | 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 | 23 | 546 | 1 | 536 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 0 | 23 | 546 | 1 | 536 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 0 | 23 | 546 | 1 | 536 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_A | 0 | 23 | 546 | 1 | 536 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1aso_B | 0 | 23 | 546 | 1 | 536 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |