Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G279600.1 |
Family | AA1 |
Protein Properties | Length: 555 Molecular Weight: 60987.9 Isoelectric Point: 8.5264 |
Chromosome | Chromosome/Scaffold: 11 Start: 61143405 End: 61146270 |
Description | Laccase/Diphenol oxidase family protein |
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 | 21 | 540 | 0 |
CRIRHYHFNVVVKNATKLCSTKPIVTVNGTFPGPRLYAREGDNVLVRLTNHVQYNVTIHWHGVRQLRTGWSDGPAYITQCPIQPGQNFLYNFTLTGQRGT LLWHAHISWLRTTVHGAIVILPKKGVPYPFPKPYKEKVIVLGEWWKADTEAVVKQATQTGLPPNISDAHTINGHPGPVPNCSSDDAYTLHVETGKTYLLR VINAAVNDELFFKIANHNLTVVEVDACYTKPFETDTLFLGPGQTTTALLKADQGIGKSLIAISPFMDTTVAVNNLTGIGYLRYNHTLAFTPTTFVAIPAV NATPVTSVFSDSLRSLNSKQYPANVPLTIDHSLFFTIGVGINPCATCFNGSRAVAAINNVSFVMPTTAILQAHYYGINGVFTDDFPAKPAIPFNYTGTPP SGVQTMNGTKVYRLAYNSTVQLVIQGNTIIAPESHPTHLHGSNFFVVGRGVGNFDPEKDPLKFNLVDPVERNTVSVPTAGWTAIRFRADNPGVWFFHCHL EVHTTWGLKMAFLVENGRGP |
Full Sequence |
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Protein Sequence Length: 555 Download |
MVCWVRTLLF ISVLVPAFVE CRIRHYHFNV VVKNATKLCS TKPIVTVNGT FPGPRLYARE 60 GDNVLVRLTN HVQYNVTIHW HGVRQLRTGW SDGPAYITQC PIQPGQNFLY NFTLTGQRGT 120 LLWHAHISWL RTTVHGAIVI LPKKGVPYPF PKPYKEKVIV LGEWWKADTE AVVKQATQTG 180 LPPNISDAHT INGHPGPVPN CSSDDAYTLH VETGKTYLLR VINAAVNDEL FFKIANHNLT 240 VVEVDACYTK PFETDTLFLG PGQTTTALLK ADQGIGKSLI AISPFMDTTV AVNNLTGIGY 300 LRYNHTLAFT PTTFVAIPAV NATPVTSVFS DSLRSLNSKQ YPANVPLTID HSLFFTIGVG 360 INPCATCFNG SRAVAAINNV SFVMPTTAIL QAHYYGINGV FTDDFPAKPA IPFNYTGTPP 420 SGVQTMNGTK VYRLAYNSTV QLVIQGNTII APESHPTHLH GSNFFVVGRG VGNFDPEKDP 480 LKFNLVDPVE RNTVSVPTAG WTAIRFRADN PGVWFFHCHL EVHTTWGLKM AFLVENGRGP 540 NESIEPPPSD LPKC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 4.0e-51 | 30 | 536 | 548 | + 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 | 1.0e-73 | 8 | 544 | 578 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-95 | 8 | 532 | 556 | + oxidoreductase | ||
TIGR03388 | ascorbase | 4.0e-101 | 23 | 532 | 544 | + 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 | 21 | 554 | 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 | CAA74103.1 | 0 | 6 | 554 | 7 | 555 | laccase [Populus trichocarpa] |
EMBL | CAC14719.1 | 0 | 6 | 554 | 7 | 555 | laccase [Populus trichocarpa] |
RefSeq | XP_002265173.1 | 0 | 5 | 554 | 5 | 553 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311202.1 | 0 | 8 | 554 | 10 | 556 | laccase [Populus trichocarpa] |
RefSeq | XP_002316233.1 | 0 | 6 | 554 | 7 | 555 | laccase 3 [Populus trichocarpa] |
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 | 544 | 1 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asq_A | 0 | 21 | 544 | 1 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_B | 0 | 21 | 544 | 1 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1asp_A | 0 | 21 | 544 | 1 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |
PDB | 1aso_B | 0 | 21 | 544 | 1 | 536 | A Chain A, Structure And Mechanisim Of Core 2 Beta1,6-N- Acetylglucosaminyltransferase: A Metal-Ion Independent Gt-A Glycosyltransferase |