y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.A01282.1 |
Family | AA1 |
Protein Properties | Length: 572 Molecular Weight: 63061.2 Isoelectric Point: 9.3008 |
Chromosome | Chromosome/Scaffold: 1 Start: 20768065 End: 20772385 |
Description | laccase 17 |
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 | 24 | 557 | 0 |
KTRHYTFHIDSHNMTRLCHTRSVLSVNKQYPGPPLVAREGDNILVKVVNHVAANVTIHWHGVRQLRTGWADGPAYVTQCPIQTNQSYTYNFTLTGQRGTL LWHAHVSWLRSSIHGPIIILPKRNESYPFEKPSKEVPIIFGEWFNVDPEAVIAQALQSGGGPNVSDAYTINGLPGPLYNCSSKDTFKLKVKPGKTYLLRL INAALNDELFFSIANHTVTVVEVDAVYTKPFSAGCLHLTPGQTMNVLLKTKTDFPNSTFLMAAWPYFTGMGTFDNSTVAGILEYEHPKSSNYPPLKKLPQ YKPTLPPMNSTGFVAKFTGQLRSLASAKFPANVPQKVDRKFFFTVGLGTSPCPKNTTCQGPNGTKFAASVNNISFVLPSVALLQAHFFGQSNGVYTTDFP TNPPVQFNYTGTPPNNTMVTNGTKTVVLAYNTSVELVMQDTSILGTESHALHLHGFNFFVVGQGSGNYNPNKDPTKFNLVDPIERNTFGVPSGGWVAIRF LADNPGVWFMHCHLDVHTSWGLKMAWIVLDGPQP |
Full Sequence |
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Protein Sequence Length: 572 Download |
MSFQNQLFIF CTLLLGFLKL AEGKTRHYTF HIDSHNMTRL CHTRSVLSVN KQYPGPPLVA 60 REGDNILVKV VNHVAANVTI HWHGVRQLRT GWADGPAYVT QCPIQTNQSY TYNFTLTGQR 120 GTLLWHAHVS WLRSSIHGPI IILPKRNESY PFEKPSKEVP IIFGEWFNVD PEAVIAQALQ 180 SGGGPNVSDA YTINGLPGPL YNCSSKDTFK LKVKPGKTYL LRLINAALND ELFFSIANHT 240 VTVVEVDAVY TKPFSAGCLH LTPGQTMNVL LKTKTDFPNS TFLMAAWPYF TGMGTFDNST 300 VAGILEYEHP KSSNYPPLKK LPQYKPTLPP MNSTGFVAKF TGQLRSLASA KFPANVPQKV 360 DRKFFFTVGL GTSPCPKNTT CQGPNGTKFA ASVNNISFVL PSVALLQAHF FGQSNGVYTT 420 DFPTNPPVQF NYTGTPPNNT MVTNGTKTVV LAYNTSVELV MQDTSILGTE SHALHLHGFN 480 FFVVGQGSGN YNPNKDPTKF NLVDPIERNT FGVPSGGWVA IRFLADNPGV WFMHCHLDVH 540 TSWGLKMAWI VLDGPQPNQK LPPPPSDLPK C* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 3.0e-46 | 38 | 145 | 110 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 7.0e-62 | 21 | 550 | 561 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-73 | 7 | 545 | 572 | + oxidoreductase | ||
TIGR03388 | ascorbase | 4.0e-76 | 25 | 545 | 553 | + 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 | 23 | 554 | 533 | + 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 | CAA74105.1 | 0 | 2 | 571 | 15 | 580 | laccase [Populus trichocarpa] |
EMBL | CAN60348.1 | 0 | 23 | 571 | 9 | 559 | hypothetical protein [Vitis vinifera] |
EMBL | CBI16224.1 | 0 | 10 | 571 | 22 | 585 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002308164.1 | 0 | 2 | 571 | 15 | 580 | laccase 110b [Populus trichocarpa] |
RefSeq | XP_002531565.1 | 0 | 8 | 571 | 18 | 577 | 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 | 24 | 562 | 2 | 532 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1asq_A | 0 | 24 | 562 | 2 | 532 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1asp_B | 0 | 24 | 562 | 2 | 532 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1asp_A | 0 | 24 | 562 | 2 | 532 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1aso_B | 0 | 24 | 562 | 2 | 532 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |