Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 327935 |
Family | AA1 |
Protein Properties | Length: 582 Molecular Weight: 66119.2 Isoelectric Point: 9.1226 |
Chromosome | Chromosome/Scaffold: 7 Start: 785491 End: 787581 |
Description | Cupredoxin superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 34 | 559 | 0 |
KIRRFKWEVKYEFKSPDCFEKLVITVNGKFPGPTIKAQQGDTIVVELKNSFMTENVAVHWHGIRQIGTPWFDGVEGVTQCPILPGEVFTYQFVVDRPGTY MYHSHYGMQRESGLIGMIQVSPPVTEPEPFTYDYDRNVLLTDWYHKSMSEKATGLASIPFKWVGEPQSLLIQGRGRFNCSNYQTTPPNLVSGVCNVSNAD CSRLILTVIPGKTYRLRIGSLTALSALSFQIEGHNLTVVEADGHYVEPFTVKNLFIYSGETYSVLLKADQNPRRNYWITTSIVSRPATTPPVAVLNYYPN HPRRRPPTPESSNLLPEWNDTRSRLAQSLAIKARRGFIHAPPENSDKVIVLLNTQNEVNGYRRWSVNNVSYHHPKTPYLIALKQNLTNAFDWRFTPPQNY DSRNYDIFAKPLNANATTSDGIYRLRFNSTVDVILQNANTMNANNSETHPWHLHGHDFWVLGYGEGKFNESEDLKRYNRVDPIMKNTVAVQPFGWTALRF RADNPGVWSFHCHIESHFFMGMGIVF |
Full Sequence |
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Protein Sequence Length: 582 Download |
MMRQKRSLDT IHVFNLMVLC FIALFSSSVL GQGKIRRFKW EVKYEFKSPD CFEKLVITVN 60 GKFPGPTIKA QQGDTIVVEL KNSFMTENVA VHWHGIRQIG TPWFDGVEGV TQCPILPGEV 120 FTYQFVVDRP GTYMYHSHYG MQRESGLIGM IQVSPPVTEP EPFTYDYDRN VLLTDWYHKS 180 MSEKATGLAS IPFKWVGEPQ SLLIQGRGRF NCSNYQTTPP NLVSGVCNVS NADCSRLILT 240 VIPGKTYRLR IGSLTALSAL SFQIEGHNLT VVEADGHYVE PFTVKNLFIY SGETYSVLLK 300 ADQNPRRNYW ITTSIVSRPA TTPPVAVLNY YPNHPRRRPP TPESSNLLPE WNDTRSRLAQ 360 SLAIKARRGF IHAPPENSDK VIVLLNTQNE VNGYRRWSVN NVSYHHPKTP YLIALKQNLT 420 NAFDWRFTPP QNYDSRNYDI FAKPLNANAT TSDGIYRLRF NSTVDVILQN ANTMNANNSE 480 THPWHLHGHD FWVLGYGEGK FNESEDLKRY NRVDPIMKNT VAVQPFGWTA LRFRADNPGV 540 WSFHCHIESH FFMGMGIVFE SGIDKVSSLP SSIMGCGQTK R* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
TIGR03390 | ascorbOXfungal | 5.0e-92 | 51 | 562 | 543 | + 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 | 7.0e-106 | 33 | 559 | 556 | + 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. |
PLN02604 | PLN02604 | 0 | 10 | 581 | 573 | + oxidoreductase |
TIGR03388 | ascorbase | 0 | 35 | 579 | 547 | + 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 | 0 | 17 | 581 | 567 | + L-ascorbate oxidase |
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 | AAY47050.1 | 0 | 26 | 581 | 26 | 574 | ascorbate oxidase [Solanum lycopersicum] |
DDBJ | BAB86897.1 | 0 | 31 | 580 | 21 | 562 | syringolide-induced protein B13-1-1 [Glycine max] |
RefSeq | NP_195693.1 | 0 | 1 | 581 | 1 | 582 | L-ascorbate oxidase, putative [Arabidopsis thaliana] |
RefSeq | XP_002306323.1 | 0 | 16 | 580 | 3 | 565 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528975.1 | 0 | 17 | 580 | 16 | 571 | l-ascorbate oxidase, 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 | 34 | 581 | 2 | 543 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
PDB | 1asq_A | 0 | 34 | 581 | 2 | 543 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
PDB | 1asp_B | 0 | 34 | 581 | 2 | 543 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
PDB | 1asp_A | 0 | 34 | 581 | 2 | 543 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
PDB | 1aso_B | 0 | 34 | 581 | 2 | 543 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |