Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.010G193100.2 |
Family | AA1 |
Protein Properties | Length: 515 Molecular Weight: 56364.7 Isoelectric Point: 9.1442 |
Chromosome | Chromosome/Scaffold: 10 Start: 18784881 End: 18787790 |
Description | Laccase/Diphenol oxidase family protein |
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 | 22 | 513 | 0 |
CKVRLYNFRVVLTNTTKLCSTKSIPTINGKFPGPTIYAREGDNVNIRLTNQVQYNVTVHWHGVRQLRTGWADGPAYITQCPIQPGQSYLYNFTLTGQRGT LLWHAHISWLRATIHGAIVIFPKKGVPYPFPKPDKEKIIILSEWWKADVEAVVNQATMTGLPPNISDAHTVNGHTGAVPGCTSPGFTLHVESGKTYLLRI INAALNDELFFKIAGHNITVVEVDATFTKPFSTDTIFIGPGQTTNALLTADKSIGKYLIAVSPFMDTVVAVDNVTAIAFLRYKGTLAFSPPVLTTTPAIN ATPATSTFMDKLRSLNSKKYPANVPLTVDHDLYFTIGVGIDPCATCTNGSKAVADINNVSFIMPTTALLQAHYYNISGVFTDDFPAKPPISFNYTGNNTA MNLKTTNGTRAYRLAFNSAVQVVLQGTTIIAPESHPFHLHGFNFFVVGKGIGNFDPDNDPKKFNLADPVERNTVSVPTAGWIAIRFKADNPG |
Full Sequence |
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Protein Sequence Length: 515 Download |
MEYYQARTML LVIFIFPALV ECKVRLYNFR VVLTNTTKLC STKSIPTING KFPGPTIYAR 60 EGDNVNIRLT NQVQYNVTVH WHGVRQLRTG WADGPAYITQ CPIQPGQSYL YNFTLTGQRG 120 TLLWHAHISW LRATIHGAIV IFPKKGVPYP FPKPDKEKII ILSEWWKADV EAVVNQATMT 180 GLPPNISDAH TVNGHTGAVP GCTSPGFTLH VESGKTYLLR IINAALNDEL FFKIAGHNIT 240 VVEVDATFTK PFSTDTIFIG PGQTTNALLT ADKSIGKYLI AVSPFMDTVV AVDNVTAIAF 300 LRYKGTLAFS PPVLTTTPAI NATPATSTFM DKLRSLNSKK YPANVPLTVD HDLYFTIGVG 360 IDPCATCTNG SKAVADINNV SFIMPTTALL QAHYYNISGV FTDDFPAKPP ISFNYTGNNT 420 AMNLKTTNGT RAYRLAFNSA VQVVLQGTTI IAPESHPFHL HGFNFFVVGK GIGNFDPDND 480 PKKFNLADPV ERNTVSVPTA GWIAIRFKAD NPGN* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam07732 | Cu-oxidase_3 | 2.0e-50 | 30 | 146 | 119 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. |
PLN02191 | PLN02191 | 3.0e-65 | 9 | 513 | 545 | + L-ascorbate oxidase |
PLN02604 | PLN02604 | 7.0e-85 | 9 | 513 | 536 | + oxidoreductase |
TIGR03388 | ascorbase | 8.0e-91 | 24 | 513 | 528 | + 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 | 22 | 513 | 497 | + 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 | CAA74103.1 | 0 | 1 | 513 | 1 | 513 | laccase [Populus trichocarpa] |
EMBL | CAC14719.1 | 0 | 1 | 513 | 1 | 513 | laccase [Populus trichocarpa] |
RefSeq | XP_002311202.1 | 0 | 1 | 513 | 1 | 514 | laccase [Populus trichocarpa] |
RefSeq | XP_002316233.1 | 0 | 1 | 513 | 1 | 513 | laccase 3 [Populus trichocarpa] |
RefSeq | XP_002530417.1 | 0 | 1 | 513 | 1 | 512 | laccase, putative [Ricinus communis] |
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 | 23 | 513 | 2 | 501 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
PDB | 1asq_A | 0 | 23 | 513 | 2 | 501 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
PDB | 1asp_B | 0 | 23 | 513 | 2 | 501 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
PDB | 1asp_A | 0 | 23 | 513 | 2 | 501 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
PDB | 1aso_B | 0 | 23 | 513 | 2 | 501 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797675 | 452 | 68 | 513 | 0 |
DT472855 | 299 | 207 | 505 | 0 |
CX664934 | 301 | 4 | 304 | 0 |
DW492091 | 290 | 3 | 291 | 0 |
EL453925 | 331 | 76 | 405 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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