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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G102700.1 |
Family | AA1 |
Protein Properties | Length: 562 Molecular Weight: 62735.1 Isoelectric Point: 8.9163 |
Chromosome | Chromosome/Scaffold: 09 Start: 9032258 End: 9034766 |
Description | laccase 11 |
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 | 27 | 548 | 0 |
AAVKRYQFDIQVKNVSRLCHAKPIVTVNGRFPGPTVYVREGDRVLVNVTNHARYNMSIHWHGLKQFRNGWADGPAYITQCPIKTGHSYTYDFNVTGQRGT LWWHAHILWLRATVYGAIVIMPKPGTPFPFPQPHREEIIIFGEWWNNDVEDIEKQGNKLGLPPNASDAHTINGKPGPLFPCSEKHTFTLEVEQAKTYLLR IINAALNDELFFAIAGHNMTVVEIDAVYTKPFTTQTILIAPGQTTNVLVQATQTPNRYFMAARPFMDAPLSIDNKTATAILQYKGIPNTVLPLLPQLPEP NDTAFARSYNAKLRSLNSPQFQANVPLIVDRHLFYTIGLGINPCPTCLNGTKLTASLNNITFVMPQIGLLQAHYFNIKGVFRLDFPDNPPTPFNYTGAPL TANLGTTLGTRVSKIAYNSTVQLVLQDTNLLTVESHPFHLHGYNFFVVGTGIGNFDPKRDPAKFNLVDPPERNTVGVPTGGWTAIRFRADNPGVWFMHCH LELHTGWGLKTAFVVENGKLPD |
Full Sequence |
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Protein Sequence Length: 562 Download |
MAAALSKKLC WASYILYLYF IYHPAEAAVK RYQFDIQVKN VSRLCHAKPI VTVNGRFPGP 60 TVYVREGDRV LVNVTNHARY NMSIHWHGLK QFRNGWADGP AYITQCPIKT GHSYTYDFNV 120 TGQRGTLWWH AHILWLRATV YGAIVIMPKP GTPFPFPQPH REEIIIFGEW WNNDVEDIEK 180 QGNKLGLPPN ASDAHTINGK PGPLFPCSEK HTFTLEVEQA KTYLLRIINA ALNDELFFAI 240 AGHNMTVVEI DAVYTKPFTT QTILIAPGQT TNVLVQATQT PNRYFMAARP FMDAPLSIDN 300 KTATAILQYK GIPNTVLPLL PQLPEPNDTA FARSYNAKLR SLNSPQFQAN VPLIVDRHLF 360 YTIGLGINPC PTCLNGTKLT ASLNNITFVM PQIGLLQAHY FNIKGVFRLD FPDNPPTPFN 420 YTGAPLTANL GTTLGTRVSK IAYNSTVQLV LQDTNLLTVE SHPFHLHGYN FFVVGTGIGN 480 FDPKRDPAKF NLVDPPERNT VGVPTGGWTA IRFRADNPGV WFMHCHLELH TGWGLKTAFV 540 VENGKLPDQS ILPPPKDLPP C* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 3.0e-52 | 36 | 543 | 547 | + 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. | ||
PLN02191 | PLN02191 | 3.0e-76 | 15 | 551 | 576 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 7.0e-86 | 8 | 547 | 582 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-94 | 29 | 549 | 571 | + 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 | 27 | 561 | 539 | + 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 | CBI32739.1 | 0 | 24 | 561 | 25 | 562 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002305436.1 | 0 | 31 | 561 | 10 | 540 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002313847.1 | 0 | 1 | 561 | 1 | 561 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512915.1 | 0 | 14 | 561 | 11 | 558 | laccase, putative [Ricinus communis] |
RefSeq | XP_002519529.1 | 0 | 14 | 561 | 12 | 559 | 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 | 27 | 551 | 1 | 536 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum In Complex With Substrate |
PDB | 1asq_A | 0 | 27 | 551 | 1 | 536 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum In Complex With Substrate |
PDB | 1asp_B | 0 | 27 | 551 | 1 | 536 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum In Complex With Substrate |
PDB | 1asp_A | 0 | 27 | 551 | 1 | 536 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum In Complex With Substrate |
PDB | 1aso_B | 0 | 27 | 551 | 1 | 536 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum In Complex With Substrate |