Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29568.m000289 |
Family | AA1 |
Protein Properties | Length: 539 Molecular Weight: 59797.6 Isoelectric Point: 9.7188 |
Chromosome | Chromosome/Scaffold: 29568 Start: 94320 End: 96332 |
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 | 27 | 530 | 0 |
TRHYKFDIKLKNVTRLCNTTTIVTVNGKSPGPRIIIREGDRLVVKVVNHSPKNVSIHWHGVRQLQTGWYDGPAYVTQCPIPPGQSYVYNFTITGQRGTLF WHAHITWLRATLYGPIIILPKLGVPYPFPKPYKQVPIIFGEWFKTDPDAIINQSLQTGGGPNVSDAYTINGLPGPLYNCSAKDTYKLKVKPGKSYLLRLI NAALNDELFISIANHTVTVVEVDATYVKPFETDKFLITPGQTMNVLLKTKPFFPKATFFMSARPYATGSGTFDNSTVAAILEYEPPAHSRLSTNQLPLLK PILPAFNDTPFAFSFSNRLRSLASAEYPATVPKTVDRRFFFTVGLGTNPCPKNQTCQGPNGTKFSASVNNISFALPTSAMLQSYFFGRSNGVYTTDFPSK PIIPFDYTGTPPNNTMVINGTKAVVLPFNTSVELVLQDTSILGNESHPLHLHGFNFYVVASGFGNFDPNNHPTKFNLIDPVERNTVGVPSGGWVAIRFQA DNPG |
Full Sequence |
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Protein Sequence Length: 539 Download |
MREKIAILLF SFLNLCLLSE LTLAGLTRHY KFDIKLKNVT RLCNTTTIVT VNGKSPGPRI 60 IIREGDRLVV KVVNHSPKNV SIHWHGVRQL QTGWYDGPAY VTQCPIPPGQ SYVYNFTITG 120 QRGTLFWHAH ITWLRATLYG PIIILPKLGV PYPFPKPYKQ VPIIFGEWFK TDPDAIINQS 180 LQTGGGPNVS DAYTINGLPG PLYNCSAKDT YKLKVKPGKS YLLRLINAAL NDELFISIAN 240 HTVTVVEVDA TYVKPFETDK FLITPGQTMN VLLKTKPFFP KATFFMSARP YATGSGTFDN 300 STVAAILEYE PPAHSRLSTN QLPLLKPILP AFNDTPFAFS FSNRLRSLAS AEYPATVPKT 360 VDRRFFFTVG LGTNPCPKNQ TCQGPNGTKF SASVNNISFA LPTSAMLQSY FFGRSNGVYT 420 TDFPSKPIIP FDYTGTPPNN TMVINGTKAV VLPFNTSVEL VLQDTSILGN ESHPLHLHGF 480 NFYVVASGFG NFDPNNHPTK FNLIDPVERN TVGVPSGGWV AIRFQADNPG EHERKVNYH 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 4.0e-51 | 33 | 147 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 8.0e-58 | 28 | 530 | 537 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 5.0e-73 | 27 | 530 | 533 | + oxidoreductase | ||
TIGR03388 | ascorbase | 3.0e-84 | 27 | 530 | 530 | + 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 | 530 | 505 | + 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 | CAN80346.1 | 0 | 5 | 530 | 12 | 543 | hypothetical protein [Vitis vinifera] |
EMBL | CBI16224.1 | 0 | 5 | 530 | 12 | 543 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284473.1 | 0 | 5 | 530 | 12 | 543 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002300066.1 | 0 | 8 | 530 | 14 | 538 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531561.1 | 0 | 1 | 539 | 1 | 539 | 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 | 530 | 4 | 501 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asq_A | 0 | 28 | 530 | 4 | 501 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_B | 0 | 28 | 530 | 4 | 501 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_A | 0 | 28 | 530 | 4 | 501 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1aso_B | 0 | 28 | 530 | 4 | 501 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |