| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_139.15 |
| Family | AA1 |
| Protein Properties | Length: 510 Molecular Weight: 56463.8 Isoelectric Point: 9.2019 |
| Chromosome | Chromosome/Scaffold: 139 Start: 84650 End: 86774 |
| Description | laccase 17 |
| 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 | 34 | 255 | 0 |
| TRHYKFDIKLQNVTRLCHTKNLVSVNGKFPGPRIVAREGDRLLIKVVNHVPNNISIHWHGIRQLRTGWADGPAYVTQCPIQTGQSYVYNYTIVGQRGTLF WHAHISWLRSTLYGPIIILPKHGVPYPFTKPHKEVPIIFGEWFNADPEAIINQALQTGGGPNVSDAYTINGLPGPLYNCSAKDTFKLKVKHGKTYLLCLI NAALNDELFFSIANHTLTVVEX | |||
| AA1 | 299 | 495 | 0 |
| XRRFFFTVGLGTNPCQHNNTCQGPNGTKFAASINNISFSMPTTALLQAHFFGQSNGVYSTKFPSAPIIPFNYTGTPPNNTMVSNGTKLVVLPFNTSVELV MQDTSILGAESHPLHLHGFNFFVVGQGFGNFDANKDPATFNLVDPVERNTVGVPSGGWVAIRFLADNPGVWFMHCHLEVHTSWGLKMAWVVLDGKLP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 510 Download |
| MGASLSPQKA FFGACLLSFI SICSLLPNPA LGITRHYKFD IKLQNVTRLC HTKNLVSVNG 60 KFPGPRIVAR EGDRLLIKVV NHVPNNISIH WHGIRQLRTG WADGPAYVTQ CPIQTGQSYV 120 YNYTIVGQRG TLFWHAHISW LRSTLYGPII ILPKHGVPYP FTKPHKEVPI IFGEWFNADP 180 EAIINQALQT GGGPNVSDAY TINGLPGPLY NCSAKDTFKL KVKHGKTYLL CLINAALNDE 240 LFFSIANHTL TVVEXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXR 300 RFFFTVGLGT NPCQHNNTCQ GPNGTKFAAS INNISFSMPT TALLQAHFFG QSNGVYSTKF 360 PSAPIIPFNY TGTPPNNTMV SNGTKLVVLP FNTSVELVMQ DTSILGAESH PLHLHGFNFF 420 VVGQGFGNFD ANKDPATFNL VDPVERNTVG VPSGGWVAIR FLADNPGVWF MHCHLEVHTS 480 WGLKMAWVVL DGKLPNQKLL PPPTDLPKC* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03388 | ascorbase | 3.0e-30 | 330 | 499 | 177 | + 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. | ||
| TIGR03388 | ascorbase | 2.0e-35 | 34 | 254 | 244 | + 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 | 9.0e-51 | 40 | 156 | 119 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| TIGR03389 | laccase | 8.0e-111 | 300 | 509 | 211 | + 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. | ||
| TIGR03389 | laccase | 8.0e-142 | 32 | 254 | 223 | + 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 |
| EMBL | CAN80346.1 | 0 | 1 | 254 | 1 | 257 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299296.1 | 0 | 1 | 254 | 1 | 253 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002299296.1 | 0 | 300 | 509 | 372 | 581 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002329138.1 | 0 | 1 | 254 | 1 | 253 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002329138.1 | 0 | 300 | 509 | 372 | 581 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3kw7_B | 2e-27 | 41 | 254 | 10 | 222 | A Chain A, Crystal Structure Of Lacb From Trametes Sp. Ah28-2 |
| PDB | 3kw7_B | 0.00000000001 | 361 | 487 | 347 | 470 | A Chain A, Crystal Structure Of Lacb From Trametes Sp. Ah28-2 |
| PDB | 3kw7_A | 2e-27 | 41 | 254 | 10 | 222 | A Chain A, Crystal Structure Of Lacb From Trametes Sp. Ah28-2 |
| PDB | 3kw7_A | 0.00000000001 | 361 | 487 | 347 | 470 | A Chain A, Crystal Structure Of Lacb From Trametes Sp. Ah28-2 |
| PDB | 1gyc_A | 4e-27 | 53 | 254 | 22 | 222 | A Chain A, Crystal Structure Determination At Room Temperature Of A Laccase From Trametes Versicolor In Its Oxidised Form Containing A Full Complement Of Copper Ions |
