Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.H03315.1 |
Family | AA1 |
Protein Properties | Length: 563 Molecular Weight: 61958.8 Isoelectric Point: 7.461 |
Chromosome | Chromosome/Scaffold: 8 Start: 48546306 End: 48548739 |
Description | laccase 11 |
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 | 28 | 555 | 0 |
AAIKKYQFDIQVKNVSRLCHAKPIVTVNGMYPGPTIYAREGDRVLINVTNHAQYNMSIHWHGLKQYRNGWADGPAYITQCPIQTGNSYTYDFNVTGQRGT LWWHAHILWLRATVHGAIVIMPPQGTPFPFPQPHSEQIILLGEWWNADVEAIEKQGNQMGLPPNMSDAHTINGKPGPLFPCSEKHTFAMEVEPGKTYLLR IINAALNDELFFAIAGHNMTVVEVDAVYAKPFSTDSILIAPGQTTNVLVQANRVPGRYFMAARSFIDAPVPVDNKTATAILQYKGIPNTVMPALAELPAP NDTAFALSYSQKLRSLNSPQFPANVPLNVSRNLFYTVGLGKNPCATCLNGTRFLASLNNISFTMPQVGLLQAHYFNTKGVFTADFPDKPPTPFNYTGAPL TANLKTSQGTRVSKIAFNSTVELVIQDTNLLTVESHPFHLHGYNFFVVGTGVGNFDPTKDPANYNLVDPMERNTVGVPTGGWTAIRFQANNPGVWFMHCH LELHTGWGLKTAFLVEDGPGPDQTVLPP |
Full Sequence |
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Protein Sequence Length: 563 Download |
MSVRGENSFL RITLLLFGFF VCFTSSEAAI KKYQFDIQVK NVSRLCHAKP IVTVNGMYPG 60 PTIYAREGDR VLINVTNHAQ YNMSIHWHGL KQYRNGWADG PAYITQCPIQ TGNSYTYDFN 120 VTGQRGTLWW HAHILWLRAT VHGAIVIMPP QGTPFPFPQP HSEQIILLGE WWNADVEAIE 180 KQGNQMGLPP NMSDAHTING KPGPLFPCSE KHTFAMEVEP GKTYLLRIIN AALNDELFFA 240 IAGHNMTVVE VDAVYAKPFS TDSILIAPGQ TTNVLVQANR VPGRYFMAAR SFIDAPVPVD 300 NKTATAILQY KGIPNTVMPA LAELPAPNDT AFALSYSQKL RSLNSPQFPA NVPLNVSRNL 360 FYTVGLGKNP CATCLNGTRF LASLNNISFT MPQVGLLQAH YFNTKGVFTA DFPDKPPTPF 420 NYTGAPLTAN LKTSQGTRVS KIAFNSTVEL VIQDTNLLTV ESHPFHLHGY NFFVVGTGVG 480 NFDPTKDPAN YNLVDPMERN TVGVPTGGWT AIRFQANNPG VWFMHCHLEL HTGWGLKTAF 540 LVEDGPGPDQ TVLPPPADLP PC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 6.0e-58 | 37 | 544 | 553 | + 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 | 1.0e-74 | 21 | 540 | 560 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 9.0e-88 | 9 | 540 | 567 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-92 | 30 | 536 | 551 | + 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 | 28 | 562 | 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 | CBI17500.1 | 0 | 25 | 562 | 5 | 542 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266464.1 | 0 | 27 | 562 | 28 | 563 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002310245.1 | 0 | 31 | 562 | 31 | 562 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002313847.1 | 0 | 13 | 562 | 13 | 561 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512915.1 | 0 | 1 | 562 | 1 | 558 | 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 | 28 | 543 | 1 | 526 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asq_A | 0 | 28 | 543 | 1 | 526 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_B | 0 | 28 | 543 | 1 | 526 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_A | 0 | 28 | 543 | 1 | 526 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1aso_B | 0 | 28 | 543 | 1 | 526 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |