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Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10000605m |
Family | AA1 |
Protein Properties | Length: 559 Molecular Weight: 61277.4 Isoelectric Point: 9.8754 |
Chromosome | Chromosome/Scaffold: 6 Start: 264060 End: 266400 |
Description | laccase 10 |
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 | 544 | 0 |
AIRKYTFNVVTKQVTRLCSTKQIVTVNGKFPGPTIYANEDDTILVNVVNNVKYNVSIHWHGIRQLRTGWADGPAYITQCPIKPGHSYVYNFTVTGQRGTL WWHAHVLWLRATVHGAIVILPKPGLPYPFPKPHREEVIILGEWWKSDTEMVINEALRSGLAPNVSDAHVINGHPGLVPNCPSQGNFKLAVESGKTYMLRL INAALNEELFFKIAGHRFTVVEVDAAYVKPFNTDTILIAPGQTTTALVSAARPSGQYLIAAAPFQDSAVVAVDNRTATATVHYSGTLSATPTKTTSPPPQ NATSVANSFVKSLRSLNSNTYPAKVPVTVDHDLLFTVGLGINRCHSCKAGNFSRVVAAINNITFKMPTTALLQAHYFNQTGVYTTDFPGRPRRVFDFTGK PPSNLATMKATKLYKLPYNATVQVVLQDTGNVAPENHPIHLHGFNFFVVGLGSGNYNSKRDSKKFNLVDPVERNTVGVPSGGWAAIRFRADNPGVWFMHC HLEVHTTWGLKMAFLVDNGKGP |
Full Sequence |
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Protein Sequence Length: 559 Download |
MEFPIRILVL FALLAFPACV HGAIRKYTFN VVTKQVTRLC STKQIVTVNG KFPGPTIYAN 60 EDDTILVNVV NNVKYNVSIH WHGIRQLRTG WADGPAYITQ CPIKPGHSYV YNFTVTGQRG 120 TLWWHAHVLW LRATVHGAIV ILPKPGLPYP FPKPHREEVI ILGEWWKSDT EMVINEALRS 180 GLAPNVSDAH VINGHPGLVP NCPSQGNFKL AVESGKTYML RLINAALNEE LFFKIAGHRF 240 TVVEVDAAYV KPFNTDTILI APGQTTTALV SAARPSGQYL IAAAPFQDSA VVAVDNRTAT 300 ATVHYSGTLS ATPTKTTSPP PQNATSVANS FVKSLRSLNS NTYPAKVPVT VDHDLLFTVG 360 LGINRCHSCK AGNFSRVVAA INNITFKMPT TALLQAHYFN QTGVYTTDFP GRPRRVFDFT 420 GKPPSNLATM KATKLYKLPY NATVQVVLQD TGNVAPENHP IHLHGFNFFV VGLGSGNYNS 480 KRDSKKFNLV DPVERNTVGV PSGGWAAIRF RADNPGVWFM HCHLEVHTTW GLKMAFLVDN 540 GKGPNQSILP PPNDLPKC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 7.0e-46 | 30 | 141 | 114 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-67 | 23 | 548 | 566 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-77 | 1 | 536 | 562 | + oxidoreductase | ||
TIGR03388 | ascorbase | 7.0e-85 | 24 | 536 | 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. | ||
TIGR03389 | laccase | 0 | 22 | 558 | 540 | + 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 | CAB69847.1 | 0 | 1 | 558 | 1 | 553 | laccase-like protein [Arabidopsis thaliana] |
RefSeq | NP_195739.2 | 0 | 1 | 558 | 1 | 558 | LAC10 (laccase 10); laccase [Arabidopsis thaliana] |
RefSeq | XP_002322961.1 | 0 | 1 | 558 | 1 | 557 | laccase 1a [Populus trichocarpa] |
RefSeq | XP_002322962.1 | 0 | 1 | 558 | 1 | 557 | laccase 1b [Populus trichocarpa] |
RefSeq | XP_002533894.1 | 0 | 1 | 558 | 1 | 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 | 24 | 536 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 0 | 24 | 536 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 0 | 24 | 536 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |