Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa003590m |
Family | AA1 |
Protein Properties | Length: 564 Molecular Weight: 62158.3 Isoelectric Point: 8.7129 |
Chromosome | Chromosome/Scaffold: 8 Start: 12160792 End: 12163068 |
Description | laccase 11 |
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 | 30 | 550 | 0 |
ALKTYQFDVQVKNVSRLCHSKPIVTVNGMFPGPTVYAREGDTLLVNVTNHAQYNMSIHWHGLKQYRNGWADGPAYITQCPIKTGHSYTYNITITGQRGTL WWHAHIFWLRATVYGAIVILPKQGTGFPFLQPYKEANIVLGEWWNNDVEEVVKQGNKLGLPPNMSDAHTINGKPGPLFPCSEKHTYALEVEQGKTYLLRI INAALNDELFFAIAGHNLTVVEIDAVYTKPFTSQAILIAPGQTTNVLVQANQVPGRYFMAARPFMDAPVSIDNKTATGILQYKGIPNTVQPVLPQLPALN NTAFALSFNAKLRSLNTAQFPASVPLKVDRHLFYTIGLGINQCTTCLNGTQLTASLNNITFVMPQIGLLQAHYFNTKGVFTTDFPDRPPTPFNYTGSPLT ANLGTKLGTRLSKLAFNSTVELVLQDTNLLTVESHPFHLHGYNFFVVGTGVGNFDPKKDPAKYNLVDPPERNTIGVPTGGWVALRFRADNPGVWFMHCHL ELHTSWGLKTAFVVENGKDSD |
Full Sequence |
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Protein Sequence Length: 564 Download |
MAKTNSFCWG SSALLFLCLV GFFSTPAKAA LKTYQFDVQV KNVSRLCHSK PIVTVNGMFP 60 GPTVYAREGD TLLVNVTNHA QYNMSIHWHG LKQYRNGWAD GPAYITQCPI KTGHSYTYNI 120 TITGQRGTLW WHAHIFWLRA TVYGAIVILP KQGTGFPFLQ PYKEANIVLG EWWNNDVEEV 180 VKQGNKLGLP PNMSDAHTIN GKPGPLFPCS EKHTYALEVE QGKTYLLRII NAALNDELFF 240 AIAGHNLTVV EIDAVYTKPF TSQAILIAPG QTTNVLVQAN QVPGRYFMAA RPFMDAPVSI 300 DNKTATGILQ YKGIPNTVQP VLPQLPALNN TAFALSFNAK LRSLNTAQFP ASVPLKVDRH 360 LFYTIGLGIN QCTTCLNGTQ LTASLNNITF VMPQIGLLQA HYFNTKGVFT TDFPDRPPTP 420 FNYTGSPLTA NLGTKLGTRL SKLAFNSTVE LVLQDTNLLT VESHPFHLHG YNFFVVGTGV 480 GNFDPKKDPA KYNLVDPPER NTIGVPTGGW VALRFRADNP GVWFMHCHLE LHTSWGLKTA 540 FVVENGKDSD HSVLPPPTDL PPC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 2.0e-55 | 38 | 548 | 553 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
PLN02191 | PLN02191 | 2.0e-72 | 14 | 542 | 564 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-88 | 13 | 541 | 564 | + oxidoreductase | ||
TIGR03388 | ascorbase | 6.0e-96 | 34 | 541 | 546 | + 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 | 29 | 563 | 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 |
EMBL | CBI32739.1 | 0 | 26 | 563 | 25 | 562 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002275392.1 | 0 | 10 | 563 | 4 | 557 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313847.1 | 0 | 2 | 563 | 4 | 561 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512915.1 | 0 | 14 | 563 | 9 | 558 | laccase, putative [Ricinus communis] |
RefSeq | XP_002519529.1 | 0 | 15 | 563 | 11 | 559 | 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 | 29 | 542 | 1 | 522 | A Chain A, Crystal Structure Of An Enoyl-coa Hydratase From Rhodobacter Sphaeroides 2.4.1 |
PDB | 1asq_A | 0 | 29 | 542 | 1 | 522 | A Chain A, Crystal Structure Of An Enoyl-coa Hydratase From Rhodobacter Sphaeroides 2.4.1 |
PDB | 1asp_B | 0 | 29 | 542 | 1 | 522 | A Chain A, Crystal Structure Of An Enoyl-coa Hydratase From Rhodobacter Sphaeroides 2.4.1 |