Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.015G040700.1 |
Family | AA1 |
Protein Properties | Length: 541 Molecular Weight: 60058.5 Isoelectric Point: 9.4444 |
Chromosome | Chromosome/Scaffold: 15 Start: 3785091 End: 3788436 |
Description | laccase 1 |
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 | 49 | 530 | 0 |
SNGDSIHIKVKNRIAQNTTLHWHGVRQLRTGWADGPAYVTQCPIRGGQSYTYKFTVTGQRGTLLWHAHYAWQRASVYGAFIIYPRIQYPFSHRIQAEIPI IFGEWWNGDPDEVEKTMLLTGGGPDSSNAYTINGLPGPLYPCSNQDTFIQTVEYGKTYLLRIINAALTNELFFAIAKHTLTVVEVVAVYTKPFATTSIMI SPGQTTTVLMTANKVPDFTGMFVMAARPYLTSVFPSNNSTTIGFLRYKNARTWKGKSPVDPSSLKLHNLPAMEDTAFATKFSDKIRSLASSQYPCNVPKT IDKRVITTISLNLQDCPENKTCSGFKGKSFFASMNNQSFVRPSISILESYYKNLTKGSFSSGFPEKPPNNFDYTVLPYGTNIEIVLQDTSFLNLENHPIH VHGHNFFIVGSGFGNFNEARDPKRYNLVDPPERNTVAVPSGGWAAIRIKADNPGVWFIHCHLEEHTSWGLATGFIVHNGQGP |
Full Sequence |
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Protein Sequence Length: 541 Download |
MEGVRKHYGI LLASLAIIAA ALPCCSSQTT RGFQFNVEWK KVTRLLTPSN GDSIHIKVKN 60 RIAQNTTLHW HGVRQLRTGW ADGPAYVTQC PIRGGQSYTY KFTVTGQRGT LLWHAHYAWQ 120 RASVYGAFII YPRIQYPFSH RIQAEIPIIF GEWWNGDPDE VEKTMLLTGG GPDSSNAYTI 180 NGLPGPLYPC SNQDTFIQTV EYGKTYLLRI INAALTNELF FAIAKHTLTV VEVVAVYTKP 240 FATTSIMISP GQTTTVLMTA NKVPDFTGMF VMAARPYLTS VFPSNNSTTI GFLRYKNART 300 WKGKSPVDPS SLKLHNLPAM EDTAFATKFS DKIRSLASSQ YPCNVPKTID KRVITTISLN 360 LQDCPENKTC SGFKGKSFFA SMNNQSFVRP SISILESYYK NLTKGSFSSG FPEKPPNNFD 420 YTVLPYGTNI EIVLQDTSFL NLENHPIHVH GHNFFIVGSG FGNFNEARDP KRYNLVDPPE 480 RNTVAVPSGG WAAIRIKADN PGVWFIHCHL EEHTSWGLAT GFIVHNGQGP SQSLLPPPPS 540 * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07731 | Cu-oxidase_2 | 8.0e-39 | 423 | 524 | 102 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-63 | 51 | 523 | 516 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 4.0e-69 | 51 | 522 | 524 | + oxidoreductase | ||
TIGR03388 | ascorbase | 6.0e-83 | 51 | 522 | 515 | + 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 | 30 | 526 | 535 | + 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 | CAN74557.1 | 0 | 1 | 538 | 1 | 570 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_173252.2 | 0 | 23 | 538 | 21 | 575 | LAC1 (Laccase 1); laccase [Arabidopsis thaliana] |
RefSeq | XP_002281603.1 | 0 | 1 | 538 | 1 | 577 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002317883.1 | 0 | 1 | 538 | 1 | 573 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002322091.1 | 0 | 1 | 538 | 1 | 573 | 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 | 51 | 534 | 41 | 536 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asq_A | 0 | 51 | 534 | 41 | 536 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asp_B | 0 | 51 | 534 | 41 | 536 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1asp_A | 0 | 51 | 534 | 41 | 536 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
PDB | 1aso_B | 0 | 51 | 534 | 41 | 536 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |