Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_139.14 |
Family | AA1 |
Protein Properties | Length: 564 Molecular Weight: 61702.9 Isoelectric Point: 9.24 |
Chromosome | Chromosome/Scaffold: 139 Start: 79681 End: 82054 |
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 | 549 | 0 |
TRHYKFDIKLQNVTRLCHTKSLVLVNGKFPGPQLVAREGMGFDSFGTGWADGPAYVTQCPIQTGQSYVYNYTIVGQRGTLFWHAHISWLRSTLYGPIIIL PKHGVPYPFTKPHKEVPIIFGEWFNADPEAIINQALQTGGGPNVSDAYTINGLPGPLYNCSAKDTFKLKVKHGKTYLLRLINAALNDELFFSIANHTLTV VEVDAGYVKPFETKTILIAPGQTTNVLLKTKPHFPNATFFMTARPYVTGQGTFDNSTVAGILEYEFPPNTIHSGVSTKNLALFKPVLPPLNDTSFATNFT NKLRSLASKEFPANVPQKVDRRFFFTVGLGTNPCQHNNTCQGPNGTKFAASINNISFSMPTTALLQAHFFGQSNGVYSANFPSAPIIPFNYTGTPPNNTM VSNGTKLVVLPFNTSVELVMQDTSILGAESHPLHLHGFNFFVVGQGFGNFDANKDPATFNLVDPVERNTVGVPSGGWVAIRFLADNPGVWFMHCHLEVHT SWGLKMAWVVSDGKLP |
Full Sequence |
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Protein Sequence Length: 564 Download |
MGASLRPRKA FFGACLLLFI SICSLLPNPA LGITRHYKFD IKLQNVTRLC HTKSLVLVNG 60 KFPGPQLVAR EGMGFDSFGT GWADGPAYVT QCPIQTGQSY VYNYTIVGQR GTLFWHAHIS 120 WLRSTLYGPI IILPKHGVPY PFTKPHKEVP IIFGEWFNAD PEAIINQALQ TGGGPNVSDA 180 YTINGLPGPL YNCSAKDTFK LKVKHGKTYL LRLINAALND ELFFSIANHT LTVVEVDAGY 240 VKPFETKTIL IAPGQTTNVL LKTKPHFPNA TFFMTARPYV TGQGTFDNST VAGILEYEFP 300 PNTIHSGVST KNLALFKPVL PPLNDTSFAT NFTNKLRSLA SKEFPANVPQ KVDRRFFFTV 360 GLGTNPCQHN NTCQGPNGTK FAASINNISF SMPTTALLQA HFFGQSNGVY SANFPSAPII 420 PFNYTGTPPN NTMVSNGTKL VVLPFNTSVE LVMQDTSILG AESHPLHLHG FNFFVVGQGF 480 GNFDANKDPA TFNLVDPVER NTVGVPSGGW VAIRFLADNP GVWFMHCHLE VHTSWGLKMA 540 WVVSDGKLPN QKIPPPPNDL PKC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00394 | Cu-oxidase | 2.0e-43 | 147 | 298 | 156 | + Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. | ||
PLN02191 | PLN02191 | 1.0e-54 | 35 | 553 | 573 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-60 | 34 | 550 | 570 | + oxidoreductase | ||
TIGR03388 | ascorbase | 7.0e-77 | 34 | 555 | 575 | + 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 | 32 | 563 | 552 | + 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 | CBI16199.1 | 0 | 20 | 563 | 1 | 566 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16224.1 | 0 | 1 | 563 | 1 | 585 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284473.1 | 0 | 1 | 563 | 1 | 585 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299296.1 | 0 | 1 | 563 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329138.1 | 0 | 1 | 563 | 1 | 581 | predicted protein [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 | 35 | 553 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asq_A | 0 | 35 | 553 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asp_B | 0 | 35 | 553 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asp_A | 0 | 35 | 553 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1aso_B | 0 | 35 | 553 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |