Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29751.m001905 |
Family | AA1 |
Protein Properties | Length: 579 Molecular Weight: 63860.3 Isoelectric Point: 8.5731 |
Chromosome | Chromosome/Scaffold: 29751 Start: 719295 End: 721942 |
Description | laccase 2 |
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 | 34 | 565 | 0 |
TRHYKFDIVMANYTRLCYTKSMVTVNGQFPGPPLIAREGDRVLVKVVNHVSNNITIHWHGVRQLQSGWADGPAYIAQCPIQTNNTFVYNFTITGQRGTLL WHAHYSALRATVYGPIIILPQLNASYPFPKPYKEVTILFGEWQNSDPEEIINQALQTGGPPNVSNAFTINGLPGPLYNCSAKDTYRLRVKPGKIYLLRII SATIDHDLFFTIANHSVTVVEADAGYIKPFKTDLLLISPGQTTNVLLETKPIAPNAKFLMLARPYSTSQGAIDNTTVAGILEYETSLNSSSKCERPIFIK PSLPPINSTAIAANYTRRFRRLVNDQFPINVPQKVDKKFFFTVGLGANPCPENQTCQGPNGTKFSASVNNNSFVLPSTAILQAYYFRKSNGVYTTDFPGV PPEPFNYTGPPPNNTFVSNGTKVMVLPFNASVEVVLQGTSILGIESHPFHLHGFNFFVVGQGFGNFDPNKDPKNYNLVDPVELNTVAVPSGGWVAIRFST DNPGVWFMHCHFDVHLSWGLDMTWLVLDGKLP |
Full Sequence |
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Protein Sequence Length: 579 Download |
MGASASLLLA FLMSLLLAMS CLLSLPQFAN AGITRHYKFD IVMANYTRLC YTKSMVTVNG 60 QFPGPPLIAR EGDRVLVKVV NHVSNNITIH WHGVRQLQSG WADGPAYIAQ CPIQTNNTFV 120 YNFTITGQRG TLLWHAHYSA LRATVYGPII ILPQLNASYP FPKPYKEVTI LFGEWQNSDP 180 EEIINQALQT GGPPNVSNAF TINGLPGPLY NCSAKDTYRL RVKPGKIYLL RIISATIDHD 240 LFFTIANHSV TVVEADAGYI KPFKTDLLLI SPGQTTNVLL ETKPIAPNAK FLMLARPYST 300 SQGAIDNTTV AGILEYETSL NSSSKCERPI FIKPSLPPIN STAIAANYTR RFRRLVNDQF 360 PINVPQKVDK KFFFTVGLGA NPCPENQTCQ GPNGTKFSAS VNNNSFVLPS TAILQAYYFR 420 KSNGVYTTDF PGVPPEPFNY TGPPPNNTFV SNGTKVMVLP FNASVEVVLQ GTSILGIESH 480 PFHLHGFNFF VVGQGFGNFD PNKDPKNYNL VDPVELNTVA VPSGGWVAIR FSTDNPGVWF 540 MHCHFDVHLS WGLDMTWLVL DGKLPNEKLP PPPSDLPKC |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07732 | Cu-oxidase_3 | 5.0e-49 | 40 | 153 | 116 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 1.0e-63 | 35 | 569 | 569 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-74 | 34 | 557 | 549 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-86 | 34 | 569 | 568 | + 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 | 32 | 579 | 549 | + 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 - 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 | 35 | 569 | 4 | 536 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asq_A | 0 | 35 | 569 | 4 | 536 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_B | 0 | 35 | 569 | 4 | 536 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1asp_A | 0 | 35 | 569 | 4 | 536 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 1aso_B | 0 | 35 | 569 | 4 | 536 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |