| Basic Information | |
|---|---|
| Species | Panicum virgatum |
| Cazyme ID | Pavirv00052149m |
| Family | AA1 |
| Protein Properties | Length: 388 Molecular Weight: 42158 Isoelectric Point: 9.1591 |
| Chromosome | Chromosome/Scaffold: 0108495 Start: 13 End: 1563 |
| Description | laccase 17 |
| 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 | 39 | 386 | 0 |
| THYYTFNVRMTNVTRLCVTKSIPTVNGQFPGPKLTAREGDRLVVKVHNHINYNVSFHWHGVRQLRNGWADGPSYITQCPIQGGQSYVYDFTVTGQRGTLW WHAHFSWLRVHLYGPLVILPKRAEGYPFPRPYKEVPILFGEWFNADTEAVINQALQTGGGPNVSDAYTFNGLPGPTYNCSARDTYNLKVKPGRTYMLRLI NSALNDELFFGIANHTLTVVEADASYVKPFTVQTLVISPGQAMNVLLTTAPSPASPAYAMAISPYTNTQGTFDNTTAAAVLEYAPMPAAAARSLPLPALP LYNDTGAVTNFSRNFRSLASAQYPAAVPLAVDRHLLFTVGLGTDPCPS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 388 Download |
| MGARHGLRRG HAASACPFIA FAAAAAVLLA LPGLAAGDTH YYTFNVRMTN VTRLCVTKSI 60 PTVNGQFPGP KLTAREGDRL VVKVHNHINY NVSFHWHGVR QLRNGWADGP SYITQCPIQG 120 GQSYVYDFTV TGQRGTLWWH AHFSWLRVHL YGPLVILPKR AEGYPFPRPY KEVPILFGEW 180 FNADTEAVIN QALQTGGGPN VSDAYTFNGL PGPTYNCSAR DTYNLKVKPG RTYMLRLINS 240 ALNDELFFGI ANHTLTVVEA DASYVKPFTV QTLVISPGQA MNVLLTTAPS PASPAYAMAI 300 SPYTNTQGTF DNTTAAAVLE YAPMPAAAAR SLPLPALPLY NDTGAVTNFS RNFRSLASAQ 360 YPAAVPLAVD RHLLFTVGLG TDPCPSNQ |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00394 | Cu-oxidase | 6.0e-35 | 171 | 287 | 121 | + Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. | ||
| PLN02604 | PLN02604 | 5.0e-38 | 55 | 287 | 259 | + oxidoreductase | ||
| TIGR03388 | ascorbase | 9.0e-41 | 55 | 287 | 256 | + 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. | ||
| pfam07732 | Cu-oxidase_3 | 4.0e-52 | 45 | 159 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| TIGR03389 | laccase | 0 | 39 | 387 | 349 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACG47007.1 | 0 | 32 | 388 | 33 | 390 | L-ascorbate oxidase precursor [Zea mays] |
| RefSeq | NP_001044776.1 | 0 | 1 | 388 | 69 | 457 | Os01g0843800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001105921.1 | 0 | 32 | 388 | 33 | 396 | putative laccase [Zea mays] |
| Swiss-Prot | Q5N9W4 | 0 | 1 | 388 | 1 | 389 | LAC5_ORYSJ RecName: Full=Putative laccase-5; AltName: Full=Benzenediol:oxygen oxidoreductase 5; AltName: Full=Urishiol oxidase 5; AltName: Full=Diphenol oxidase 5; Flags: Precursor |
| RefSeq | XP_002456622.1 | 0 | 1 | 388 | 1 | 387 | hypothetical protein SORBIDRAFT_03g039570 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 5e-35 | 41 | 375 | 5 | 349 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asq_A | 5e-35 | 41 | 375 | 5 | 349 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asp_B | 5e-35 | 41 | 375 | 5 | 349 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asp_A | 5e-35 | 41 | 375 | 5 | 349 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1aso_B | 5e-35 | 41 | 375 | 5 | 349 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
