| Basic Information | |
|---|---|
| Species | Setaria italica |
| Cazyme ID | Si001174m |
| Family | AA1 |
| Protein Properties | Length: 496 Molecular Weight: 50872.6 Isoelectric Point: 6.3333 |
| Chromosome | Chromosome/Scaffold: 5 Start: 41558050 End: 41560008 |
| Description | laccase 12 |
| 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 | 3 | 383 | 0 |
| STGEWWNRNVVDVENDAILSGQLPTQSDAFTVNGKTGLLYQCANETFTAVVEPNTRVLLRVINAGLNSHLFFKVAGHNFTVVAVDGSYTSNLNTDTLVIA PGQTVDALVTTSAAPGSYYMAVLAHDTMSPLAFAASDTTTATAILQYNGTSTNPPAMPVMPSSSDSATANAFYFGLRGLGTPAVPSPVDVSMTIELGLGQ LPCDPSQTKCNGTAAAAAMNGVSFRLPAPETSLLGAHLNGLTGVFTADFPDGPPPSGTAMAVGTKVKKLAYNSVVEIVLQNPSAVPTENHPIHLHGFNFF VLAQGVGTFTPGSASYNLVDPVARNTIAVPGGGWAVIRFVANNPGMWFFHCHLDPHVPMGLGMVFHVDSGTTAGATLPPPP | |||
| Full Sequence |
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| Protein Sequence Length: 496 Download |
| MSSTGEWWNR NVVDVENDAI LSGQLPTQSD AFTVNGKTGL LYQCANETFT AVVEPNTRVL 60 LRVINAGLNS HLFFKVAGHN FTVVAVDGSY TSNLNTDTLV IAPGQTVDAL VTTSAAPGSY 120 YMAVLAHDTM SPLAFAASDT TTATAILQYN GTSTNPPAMP VMPSSSDSAT ANAFYFGLRG 180 LGTPAVPSPV DVSMTIELGL GQLPCDPSQT KCNGTAAAAA MNGVSFRLPA PETSLLGAHL 240 NGLTGVFTAD FPDGPPPSGT AMAVGTKVKK LAYNSVVEIV LQNPSAVPTE NHPIHLHGFN 300 FFVLAQGVGT FTPGSASYNL VDPVARNTIA VPGGGWAVIR FVANNPGMWF FHCHLDPHVP 360 MGLGMVFHVD SGTTAGATLP PPPADWVGVC DAQNYATAAA AAAAATPAPV PAPAPAPTLA 420 PGSAPAAATS PRAAAGSPVK PSSPVDHKPS PNLPQRRGDG RPSATSAAAE PRATGHLTCL 480 LCTIILFFVL HEHKA* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02604 | PLN02604 | 8.0e-38 | 43 | 367 | 350 | + oxidoreductase | ||
| PLN02191 | PLN02191 | 2.0e-38 | 43 | 367 | 339 | + L-ascorbate oxidase | ||
| pfam07731 | Cu-oxidase_2 | 1.0e-39 | 243 | 370 | 128 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| TIGR03388 | ascorbase | 6.0e-46 | 43 | 367 | 345 | + 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 | 1.0e-123 | 5 | 370 | 385 | + 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 | AAL73970.1 | 0 | 5 | 385 | 178 | 559 | AF465470_1 laccase LAC5-4 [Lolium perenne] |
| GenBank | EEC71811.1 | 0 | 5 | 385 | 169 | 555 | hypothetical protein OsI_04449 [Oryza sativa Indica Group] |
| RefSeq | NP_001044815.1 | 0 | 5 | 385 | 169 | 555 | Os01g0850700 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001105789.1 | 0 | 5 | 495 | 163 | 641 | laccase 1 [Zea mays] |
| RefSeq | XP_002456640.1 | 0 | 5 | 495 | 163 | 649 | hypothetical protein SORBIDRAFT_03g039970 [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 | 3e-35 | 44 | 367 | 201 | 521 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1asq_A | 3e-35 | 44 | 367 | 201 | 521 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1asp_B | 3e-35 | 44 | 367 | 201 | 521 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1asp_A | 3e-35 | 44 | 367 | 201 | 521 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| PDB | 1aso_B | 3e-35 | 44 | 367 | 201 | 521 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| FL858886 | 246 | 11 | 256 | 0 |
| CK206548 | 318 | 4 | 318 | 0 |
| CA121046 | 238 | 158 | 395 | 0 |
| DY619130 | 212 | 5 | 215 | 0 |
| CO468970 | 212 | 5 | 215 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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