| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s17_180V6.1 |
| Family | AA1 |
| Protein Properties | Length: 565 Molecular Weight: 62543.9 Isoelectric Point: 9.8964 |
| Chromosome | Chromosome/Scaffold: 17 Start: 1220334 End: 1223811 |
| Description | laccase 12 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA1 | 31 | 546 | 0 |
| KTHHLNWTVENKRVTRNCATVDIPTVNGRFPGPTIEVNEGDTLVIKVTNKQQYPVTLHWHGIKQFRTNYADGPAHITQCPIQPNKSYIYEFTLNDQRGTF FWHAHINWMRSTVHGALIVHPKKKAPYGAVAGEIPIIMGEFFGLHPNVVELGFINTLAPVENRTTLASTINGFPGPFFNCSSATKVYKVKKGKTYLLRII DAALNSDHYFAVANHSVTVVAADGNYLKPFKTSYVPMSPGQTTDVLIKFDKPCGRYYFGMNAGPVPAVGAPPPFVPAVSIFQYEGADSTTSPVVPVFPDR FNLAPLNAYHAKLKNLNRYHLPRKVDKSFLYVVGISSVNCIPSENCTRKIAGTMQNMTFDDPVGTSILEAYASGAKGVYTTDFPAQPPSLNVNTTRPDPH YLAGNRGTRLRELKFGSVVQVVLQNFFAFGVLDHPFHLHGHDFYVVGQNYGVYDPVQSPKTFNLKDPPLFNTIGVPNGGWVALRFKANNPGVWLLHCHFE RHKSWGMHQVFITRNG | |||
| Full Sequence |
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| Protein Sequence Length: 565 Download |
| MASMKMSSFK VLCFIAIIVA VFTQKAVATS KTHHLNWTVE NKRVTRNCAT VDIPTVNGRF 60 PGPTIEVNEG DTLVIKVTNK QQYPVTLHWH GIKQFRTNYA DGPAHITQCP IQPNKSYIYE 120 FTLNDQRGTF FWHAHINWMR STVHGALIVH PKKKAPYGAV AGEIPIIMGE FFGLHPNVVE 180 LGFINTLAPV ENRTTLASTI NGFPGPFFNC SSATKVYKVK KGKTYLLRII DAALNSDHYF 240 AVANHSVTVV AADGNYLKPF KTSYVPMSPG QTTDVLIKFD KPCGRYYFGM NAGPVPAVGA 300 PPPFVPAVSI FQYEGADSTT SPVVPVFPDR FNLAPLNAYH AKLKNLNRYH LPRKVDKSFL 360 YVVGISSVNC IPSENCTRKI AGTMQNMTFD DPVGTSILEA YASGAKGVYT TDFPAQPPSL 420 NVNTTRPDPH YLAGNRGTRL RELKFGSVVQ VVLQNFFAFG VLDHPFHLHG HDFYVVGQNY 480 GVYDPVQSPK TFNLKDPPLF NTIGVPNGGW VALRFKANNP GVWLLHCHFE RHKSWGMHQV 540 FITRNGVGKS QTLPGPKHPL PKCT* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03390 | ascorbOXfungal | 1.0e-42 | 39 | 542 | 552 | + 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. | ||
| pfam07732 | Cu-oxidase_3 | 5.0e-47 | 38 | 153 | 118 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
| PLN02191 | PLN02191 | 5.0e-65 | 14 | 542 | 568 | + L-ascorbate oxidase | ||
| TIGR03388 | ascorbase | 2.0e-73 | 32 | 554 | 573 | + 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 | 31 | 563 | 545 | + 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 |
| RefSeq | NP_196158.1 | 0 | 8 | 563 | 6 | 565 | LAC12 (laccase 12); laccase [Arabidopsis thaliana] |
| RefSeq | XP_001755400.1 | 0 | 1 | 564 | 1 | 564 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001766678.1 | 0 | 24 | 563 | 24 | 570 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002277722.1 | 0 | 26 | 563 | 28 | 574 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315131.1 | 0 | 14 | 563 | 15 | 575 | laccase 90c [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 30 | 554 | 1 | 532 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| PDB | 1asq_A | 0 | 30 | 554 | 1 | 532 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| PDB | 1asp_B | 0 | 30 | 554 | 1 | 532 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| PDB | 1asp_A | 0 | 30 | 554 | 1 | 532 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| PDB | 1aso_B | 0 | 30 | 554 | 1 | 532 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| Signal Peptide | |||||
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| Cleavage Site | |||||
| 28 | |||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| EE591979 | 594 | 10 | 557 | 0 |
| HO797675 | 502 | 76 | 563 | 0 |
| BJ171968 | 165 | 401 | 565 | 0 |
| BJ605527 | 167 | 399 | 565 | 0 |
| BJ606616 | 160 | 406 | 565 | 0 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Physcomitrella patens | Pp1s175_122V6.1 | Pp1s17_180V6.2 | Pp1s86_61V6.2 | Pp1s86_61V6.1 | |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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