Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29568.m000293 |
Family | AA1 |
Protein Properties | Length: 577 Molecular Weight: 63727.9 Isoelectric Point: 9.7632 |
Chromosome | Chromosome/Scaffold: 29568 Start: 130228 End: 132831 |
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 | 33 | 563 | 0 |
VTRHYTFNIVNQTITRLCHTRSVLTVNGKFPGPRLVAREGDRVIIKVVNHVSSNVTIHWHGIRQLTTGWADGPAYITQCPIQTGQSYTYNFTITGQRGTL LWHAHISWLRSSLYGPIIIFPRRNESYPFQKPYKEIPILLGEWFNVDPEAVIAQALQIGAGPNVSDAYTINGLPGPLYNCSSKDTFKLKVKPGKTYLLRI INAALNDELFFSIASHTLTVVEADAIYTKPFETDTLLITPGQTTNVLLKTKPSLPNATYLMAARPYFTGQGTFDNSTAAAILEYKHPSNISRQLPLFKPT LPPINATGFVANITRRFRSLANAKFPANVPQNVDRKFFFTVGLGTNPCPANTTCQGPTNTTKFSASINNVSFLMPSVSLLQSYYFGKSNGIFTADFPQNP PTPFNYTGTPPNNTNVSNGTRALMLRFNTSVELVMQDTSILGAESHPLHLHGFNFFVVGQGFGNYNSNKDPANFNLVDPMERNTVGVPAGGWVAIRFLAD NPGVWFMHCHLDVHTSWGLRMAWLVLNGPQP |
Full Sequence |
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Protein Sequence Length: 577 Download |
MGNSHRSSFP SMAAALAFTF CILSLLPNFA VAVTRHYTFN IVNQTITRLC HTRSVLTVNG 60 KFPGPRLVAR EGDRVIIKVV NHVSSNVTIH WHGIRQLTTG WADGPAYITQ CPIQTGQSYT 120 YNFTITGQRG TLLWHAHISW LRSSLYGPII IFPRRNESYP FQKPYKEIPI LLGEWFNVDP 180 EAVIAQALQI GAGPNVSDAY TINGLPGPLY NCSSKDTFKL KVKPGKTYLL RIINAALNDE 240 LFFSIASHTL TVVEADAIYT KPFETDTLLI TPGQTTNVLL KTKPSLPNAT YLMAARPYFT 300 GQGTFDNSTA AAILEYKHPS NISRQLPLFK PTLPPINATG FVANITRRFR SLANAKFPAN 360 VPQNVDRKFF FTVGLGTNPC PANTTCQGPT NTTKFSASIN NVSFLMPSVS LLQSYYFGKS 420 NGIFTADFPQ NPPTPFNYTG TPPNNTNVSN GTRALMLRFN TSVELVMQDT SILGAESHPL 480 HLHGFNFFVV GQGFGNYNSN KDPANFNLVD PMERNTVGVP AGGWVAIRFL ADNPGVWFMH 540 CHLDVHTSWG LRMAWLVLNG PQPNQKLQPP PSDLPKC |
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-52 | 40 | 154 | 117 | + Multicopper oxidase. This entry contains many divergent copper oxidase-like domains that are not recognised by the pfam00394 model. | ||
PLN02191 | PLN02191 | 3.0e-67 | 12 | 551 | 570 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 1.0e-81 | 12 | 553 | 575 | + oxidoreductase | ||
TIGR03388 | ascorbase | 2.0e-91 | 34 | 551 | 554 | + 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 | 577 | 547 | + 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 | CAA74105.1 | 0 | 1 | 577 | 1 | 580 | laccase [Populus trichocarpa] |
RefSeq | XP_002299296.1 | 0 | 1 | 577 | 1 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300066.1 | 0 | 10 | 577 | 8 | 580 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002308164.1 | 0 | 1 | 577 | 1 | 580 | laccase 110b [Populus trichocarpa] |
RefSeq | XP_002531565.1 | 0 | 1 | 577 | 1 | 577 | 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 | 35 | 551 | 4 | 517 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asq_A | 0 | 35 | 551 | 4 | 517 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_B | 0 | 35 | 551 | 4 | 517 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1asp_A | 0 | 35 | 551 | 4 | 517 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 1aso_B | 0 | 35 | 551 | 4 | 517 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |