y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra040902 |
Family | AA1 |
Protein Properties | Length: 573 Molecular Weight: 64345.6 Isoelectric Point: 8.8544 |
Chromosome | Chromosome/Scaffold: 000302 Start: 27658 End: 29945 |
Description | Plant L-ascorbate oxidase |
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 | 333 | 545 | 5.9e-40 |
PRWDDYNRSISFSNKFFAAKGYPPPPEKSDEQLYLLNTQNLIDGHTKWAINNVSLSVTATPYIGAIRYGLNTLSYLKSPAKELVKSYDITKPPVNPTTTK SSGIYKFPMGIVVDVILQNANVLKGKISEIHPWHLHGHDFWVLGYGDGKFRPGVDEKKYNLKNPPLRNTVALYPFGWTALRFVTDNPGVWFFHCHIEPHL HMGMGVVFAEGVD | |||
AA1 | 79 | 327 | 0 |
IHWHGIRQRGTPWSDGAAGVTQCPINPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGMMIVRSPKEKLRYDGEFNLLLSDWWHQSTHSQELALSSSPM RWIGEPQSLLINGRGQFNCSQAAYLSNEGKRQCTFRKNDQCAPETLRVRPNKVYRLRIASTTALASLNLAVEGHKLEVVEADGNYVKPFTVDDIDIYSGE TYSVLLRTHSFPTKKHFISVGVRGRKPNTTQALTVLSYIDAPESARPSL |
Full Sequence |
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Protein Sequence Length: 573 Download |
MSVIVWWLVT VVLVAVHSAS ARVVELDWEV EYKFWWPDCK EGIVMAINGQ FPGPTIDAVA 60 GDIVIIHLTN KLSTEGVVIH WHGIRQRGTP WSDGAAGVTQ CPINPGETFT YNFTVDKPGT 120 HFYHGHYGMQ RSAGLYGMMI VRSPKEKLRY DGEFNLLLSD WWHQSTHSQE LALSSSPMRW 180 IGEPQSLLIN GRGQFNCSQA AYLSNEGKRQ CTFRKNDQCA PETLRVRPNK VYRLRIASTT 240 ALASLNLAVE GHKLEVVEAD GNYVKPFTVD DIDIYSGETY SVLLRTHSFP TKKHFISVGV 300 RGRKPNTTQA LTVLSYIDAP ESARPSLPPP VTPRWDDYNR SISFSNKFFA AKGYPPPPEK 360 SDEQLYLLNT QNLIDGHTKW AINNVSLSVT ATPYIGAIRY GLNTLSYLKS PAKELVKSYD 420 ITKPPVNPTT TKSSGIYKFP MGIVVDVILQ NANVLKGKIS EIHPWHLHGH DFWVLGYGDG 480 KFRPGVDEKK YNLKNPPLRN TVALYPFGWT ALRFVTDNPG VWFFHCHIEP HLHMGMGVVF 540 AEGVDRIAKM DIPDEVLGCG LTRKWLMNQG RH* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-74 | 39 | 543 | 541 | + 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. | ||
TIGR03389 | laccase | 2.0e-98 | 39 | 540 | 528 | + 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. | ||
PLN02191 | PLN02191 | 0 | 25 | 571 | 551 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 0 | 25 | 562 | 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. | ||
PLN02604 | PLN02604 | 0 | 28 | 563 | 541 | + oxidoreductase |
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 | AAF20931.1 | 0 | 1 | 572 | 2 | 574 | AF206721_1 ascorbate oxidase [Brassica juncea] |
GenBank | AAK91422.1 | 0 | 45 | 572 | 1 | 530 | AT5g21100/T10F18_130 [Arabidopsis thaliana] |
DDBJ | BAA20519.1 | 0 | 8 | 572 | 1 | 567 | ascorbate oxidase [Arabidopsis thaliana] |
RefSeq | NP_197609.1 | 0 | 25 | 571 | 25 | 572 | L-ascorbate oxidase, putative [Arabidopsis thaliana] |
RefSeq | NP_680176.5 | 0 | 25 | 572 | 39 | 588 | L-ascorbate oxidase/ copper ion binding / oxidoreductase [Arabidopsis thaliana] |
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 | 21 | 572 | 1 | 551 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asq_A | 0 | 21 | 572 | 1 | 551 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_B | 0 | 21 | 572 | 1 | 551 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_A | 0 | 21 | 572 | 1 | 551 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1aso_B | 0 | 21 | 572 | 1 | 551 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |