y
Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10000569m |
Family | AA1 |
Protein Properties | Length: 576 Molecular Weight: 64413.4 Isoelectric Point: 8.9562 |
Chromosome | Chromosome/Scaffold: 6 Start: 7199544 End: 7203604 |
Description | Plant L-ascorbate oxidase |
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 | 338 | 548 | 8.70206e-43 |
PRWDDFERSKNFSKKIFSAMGSPPPPKKYRKRLILLNTQNLIDGYTKWAINNVSLMTPATPYLGSVKYNLKLGFNRKSPPKTYRFDYDIMNPPPFPNTTT GNGIYVFPFNVTVDVILQNSNVLKGVVSEIHPWHLHGHDFWVLGYGDGKFKPGVDEKTYNLKNPPLRNTAILYPYGWTALRFVTDNPGVWFFHCHIEPHL HMGMGVVFAEG | |||
AA1 | 76 | 336 | 0 |
IHWHGIRQLGSPWADGAAGVTQCAINPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGQRERLRYDGEFNLLLSDWWHEPISSQELGLSS KPMRWIGEAQSILINGRGQFNCSLAAQFSNNNNNTSSLPMCTFKEGDQCAPQKLHVEPNKTYRIRLASTTALASLNLAIQGHKLVVVEADANYVTPFTTD DIDIYSGESYSVLLTTDQDPSQNYYISVGVRGRKPNTNQALTILNYVTAPASKLPSSPPPV |
Full Sequence |
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Protein Sequence Length: 576 Download |
MGLWWIVVVA VLANTASAAV REYHWEVEYK FWWPDCNEGA VMTVNGQFPG PTIKAVAGDT 60 IVVHLTNKLT TEGLVIHWHG IRQLGSPWAD GAAGVTQCAI NPGETFTYKF TVEKPGTHFY 120 HGHYGMQRSA GLYGSLIVDV AKGQRERLRY DGEFNLLLSD WWHEPISSQE LGLSSKPMRW 180 IGEAQSILIN GRGQFNCSLA AQFSNNNNNT SSLPMCTFKE GDQCAPQKLH VEPNKTYRIR 240 LASTTALASL NLAIQGHKLV VVEADANYVT PFTTDDIDIY SGESYSVLLT TDQDPSQNYY 300 ISVGVRGRKP NTNQALTILN YVTAPASKLP SSPPPVTPRW DDFERSKNFS KKIFSAMGSP 360 PPPKKYRKRL ILLNTQNLID GYTKWAINNV SLMTPATPYL GSVKYNLKLG FNRKSPPKTY 420 RFDYDIMNPP PFPNTTTGNG IYVFPFNVTV DVILQNSNVL KGVVSEIHPW HLHGHDFWVL 480 GYGDGKFKPG VDEKTYNLKN PPLRNTAILY PYGWTALRFV TDNPGVWFFH CHIEPHLHMG 540 MGVVFAEGLN RIGKIPDEAL GCGLTKQYLM NRHRG* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 1.0e-70 | 36 | 548 | 549 | + 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 | 1.0e-101 | 18 | 560 | 563 | + 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 | 1 | 574 | 575 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 0 | 20 | 565 | 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. | ||
PLN02604 | PLN02604 | 0 | 3 | 566 | 569 | + 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 | AAF20932.1 | 0 | 4 | 573 | 1 | 572 | AF206722_1 ascorbate oxidase [Brassica juncea] |
GenBank | AAF20933.1 | 0 | 5 | 573 | 1 | 571 | AF206723_1 ascorbate oxidase [Brassica juncea] |
GenBank | AAK91422.1 | 0 | 42 | 574 | 1 | 529 | AT5g21100/T10F18_130 [Arabidopsis thaliana] |
DDBJ | BAA20519.1 | 0 | 6 | 574 | 2 | 566 | ascorbate oxidase [Arabidopsis thaliana] |
RefSeq | NP_680176.5 | 0 | 21 | 574 | 38 | 587 | 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 | 18 | 571 | 1 | 547 | I Chain I, Promiscuous Behavior Of Proteins In Archaeal Ribosomes Revealed By Cryo-em: Implications For Evolution Of Eukaryotic Ribosomes (50s Ribosomal Protei |
PDB | 1asq_A | 0 | 18 | 571 | 1 | 547 | I Chain I, Promiscuous Behavior Of Proteins In Archaeal Ribosomes Revealed By Cryo-em: Implications For Evolution Of Eukaryotic Ribosomes (50s Ribosomal Protei |
PDB | 1asp_B | 0 | 18 | 571 | 1 | 547 | I Chain I, Promiscuous Behavior Of Proteins In Archaeal Ribosomes Revealed By Cryo-em: Implications For Evolution Of Eukaryotic Ribosomes (50s Ribosomal Protei |
PDB | 1asp_A | 0 | 18 | 571 | 1 | 547 | I Chain I, Promiscuous Behavior Of Proteins In Archaeal Ribosomes Revealed By Cryo-em: Implications For Evolution Of Eukaryotic Ribosomes (50s Ribosomal Protei |
PDB | 1aso_B | 0 | 18 | 571 | 1 | 547 | I Chain I, Promiscuous Behavior Of Proteins In Archaeal Ribosomes Revealed By Cryo-em: Implications For Evolution Of Eukaryotic Ribosomes (50s Ribosomal Protei |