Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30004.m000427 |
Family | AA1 |
Protein Properties | Length: 580 Molecular Weight: 64208.8 Isoelectric Point: 9.191 |
Chromosome | Chromosome/Scaffold: 30004 Start: 412392 End: 414693 |
Description | laccase 17 |
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 | 32 | 566 | 0 |
VTRDYEFNIMLQNVTRLCHSKSMVTVNGQFPGPRIMAREGDRLLIKVVNNVQNNISIHWHGIRQLRSGWADGPAYIAQCPIQTGQSYVYNYTIIGQRGTL WWHAHISWLRSTLYGPLIILPKHGVPYPFAKPYKEVSIVFGEWFNADTEAVIKQALQTGGGPNVSDAYTINGLPGPLYNCSAKDTFRLKVKLGKTYLLRI INAALNDELFFSIANHTMKVVEVDAVYVKPFDTKTILISPGQTTNVLLKTKLHYPNATFLMTARPYVTGQGTFDNSTVAGILEYEPSQKTHHSLSINKLQ FFKPKLPVLNDTSFATKFSSQLRSLDSAEFPANVPQKVDKQFFFTVGLGTSPCPKNQTCQGPNGTMFAASVNNVSFDMPDIALLQAHFSGQSNGVYNPNF PSSPLFPFNYTGNPPNNTMVSSGTKVVVLPFNTSVELIMQDTSILGAESHPLHLHGFNFFVVGQGFGNFDRNKDPTKFNLVDPVERNTVGVPSGGWVAVR FLADNPGVWFMHCHLEVHTSWGLKMAWVVLDGKLP |
Full Sequence |
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Protein Sequence Length: 580 Download |
MGVSLLTSPS FLGTFLLSFI TLCLHPNPAL AVTRDYEFNI MLQNVTRLCH SKSMVTVNGQ 60 FPGPRIMARE GDRLLIKVVN NVQNNISIHW HGIRQLRSGW ADGPAYIAQC PIQTGQSYVY 120 NYTIIGQRGT LWWHAHISWL RSTLYGPLII LPKHGVPYPF AKPYKEVSIV FGEWFNADTE 180 AVIKQALQTG GGPNVSDAYT INGLPGPLYN CSAKDTFRLK VKLGKTYLLR IINAALNDEL 240 FFSIANHTMK VVEVDAVYVK PFDTKTILIS PGQTTNVLLK TKLHYPNATF LMTARPYVTG 300 QGTFDNSTVA GILEYEPSQK THHSLSINKL QFFKPKLPVL NDTSFATKFS SQLRSLDSAE 360 FPANVPQKVD KQFFFTVGLG TSPCPKNQTC QGPNGTMFAA SVNNVSFDMP DIALLQAHFS 420 GQSNGVYNPN FPSSPLFPFN YTGNPPNNTM VSSGTKVVVL PFNTSVELIM QDTSILGAES 480 HPLHLHGFNF FVVGQGFGNF DRNKDPTKFN LVDPVERNTV GVPSGGWVAV RFLADNPGVW 540 FMHCHLEVHT SWGLKMAWVV LDGKLPNQKL LPPPADLPKC |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 9.0e-51 | 44 | 155 | 114 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 2.0e-59 | 15 | 570 | 589 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-73 | 16 | 567 | 581 | + oxidoreductase | ||
TIGR03388 | ascorbase | 4.0e-79 | 33 | 570 | 576 | + 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 | 31 | 580 | 551 | + 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 |
RefSeq | XP_002284473.1 | 0 | 1 | 580 | 1 | 585 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299296.1 | 0 | 1 | 580 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329138.1 | 0 | 1 | 580 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520231.1 | 0 | 1 | 580 | 1 | 580 | laccase, putative [Ricinus communis] |
RefSeq | XP_002531824.1 | 0 | 5 | 580 | 6 | 576 | 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 | 34 | 570 | 4 | 536 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asq_A | 0 | 34 | 570 | 4 | 536 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_B | 0 | 34 | 570 | 4 | 536 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1asp_A | 0 | 34 | 570 | 4 | 536 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1aso_B | 0 | 34 | 570 | 4 | 536 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |