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Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra018408 |
Family | AA1 |
Protein Properties | Length: 579 Molecular Weight: 64231.9 Isoelectric Point: 9.8106 |
Chromosome | Chromosome/Scaffold: 05 Start: 8020717 End: 8022967 |
Description | laccase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 29 | 564 | 0 |
TRHYTFHIQLKNITRLCKTKSIVAVNGKFPGPKVTAREGDNLQIKVVNHVSNNISIHWHGIRQLRSGWADGPSYVTQCPIQTGQSYVYNFTIIGQRGTLW WHAHIQWMRATVYGPLIILPKLYQHYPFPKPYKQVPIIFGEWFNADPQAVVQQALQTGAGPNASDAHTFNGLPGPLYNCSTKDTYKLVVKPGKTYLLRLI NAALDDELFFTIANHTLTVVEADASYVKPFQTNIVLLGPGQTTNVLLKTKPIYPNATFYMLARPYFTGQGTIDNTTVAGILKYHHKPTSNHFNSSKNLPV INPSLPPINSTSYAANFTKMFRSLANSRFPANVPKIVDKKFFFTVGLGTNPCPKNQTCQGPTNTTKFAAAINNVTFILPNTTSLLQSYFSGMSKKVFTTN FPSAPVFPFNYTGVPPNNTMVSGGTKVVVLKYNTTVELVLQGTSILGIEAHPIHLHGYNFYVVGQGFGNFDPTRDPKQYNLVDPVERNTINVPSGGWVAI RFLADNPGVWFMHCHIEIHLSWGLTMAWVVLDGDLP |
Full Sequence |
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Protein Sequence Length: 579 Download |
MAMWGLHYLL VAFLITITYG INAESAGITR HYTFHIQLKN ITRLCKTKSI VAVNGKFPGP 60 KVTAREGDNL QIKVVNHVSN NISIHWHGIR QLRSGWADGP SYVTQCPIQT GQSYVYNFTI 120 IGQRGTLWWH AHIQWMRATV YGPLIILPKL YQHYPFPKPY KQVPIIFGEW FNADPQAVVQ 180 QALQTGAGPN ASDAHTFNGL PGPLYNCSTK DTYKLVVKPG KTYLLRLINA ALDDELFFTI 240 ANHTLTVVEA DASYVKPFQT NIVLLGPGQT TNVLLKTKPI YPNATFYMLA RPYFTGQGTI 300 DNTTVAGILK YHHKPTSNHF NSSKNLPVIN PSLPPINSTS YAANFTKMFR SLANSRFPAN 360 VPKIVDKKFF FTVGLGTNPC PKNQTCQGPT NTTKFAAAIN NVTFILPNTT SLLQSYFSGM 420 SKKVFTTNFP SAPVFPFNYT GVPPNNTMVS GGTKVVVLKY NTTVELVLQG TSILGIEAHP 480 IHLHGYNFYV VGQGFGNFDP TRDPKQYNLV DPVERNTINV PSGGWVAIRF LADNPGVWFM 540 HCHIEIHLSW GLTMAWVVLD GDLPNQKLPP PPSDFPTC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR03390 | ascorbOXfungal | 1.0e-50 | 32 | 562 | 575 | + 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 | 6.0e-70 | 9 | 557 | 584 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 3.0e-78 | 6 | 552 | 584 | + oxidoreductase | ||
TIGR03388 | ascorbase | 7.0e-89 | 29 | 552 | 561 | + 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 | 578 | 553 | + 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 |
GenBank | ABW74558.1 | 0 | 1 | 578 | 1 | 573 | putative laccase [Boechera divaricarpa] |
GenBank | ABW81073.1 | 0 | 15 | 578 | 1 | 563 | unknown [Cleome spinosa] |
GenBank | ABW81166.1 | 0 | 1 | 578 | 1 | 573 | unknown [Capsella rubella] |
EMBL | CBI31651.1 | 0 | 23 | 578 | 539 | 1094 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_180477.1 | 0 | 1 | 578 | 1 | 573 | LAC2 (laccase 2); laccase [Arabidopsis thaliana] |
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 | 30 | 568 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asq_A | 0 | 30 | 568 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asp_B | 0 | 30 | 568 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1asp_A | 0 | 30 | 568 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1aso_B | 0 | 30 | 568 | 4 | 536 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |