y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.012G111900.1 |
Family | AA1 |
Protein Properties | Length: 557 Molecular Weight: 60778.8 Isoelectric Point: 9.619 |
Chromosome | Chromosome/Scaffold: 12 Start: 25401053 End: 25403534 |
Description | Laccase/Diphenol oxidase family protein |
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 | 21 | 542 | 0 |
CTVRHYKFNVVMKNTTRLCSSKPIVSVNGKFPGPTLYAREGDTVLVKVVNHVKYNVSIHWHGIRQLRTGWADGPAYITQCPIQSGQSYVYNFTITGQRGT LLWHAHILWLRSTVHGAIVILPKRGVPYPFPKPHKEVVVVLAEWWKSDTEAVINEALKSGLAPNVSDAHTINGHPGRVSGCPSQGGFSLPVESGKTYLLR LINAALNEELFFKIAGHKLTVVEVDATYVKPFKIDTVVIAPGQTTNVLVSADQNSGKYMVAASPFMDAPVAVDNLTATATLHYSGTLDNTPTSLTTPPPQ NATSVANNFIDSLRSLNSKQFPALVPRTIDHNLYFTVGLGINPCPTCKAGNGSRVVASINNVTFTMPTTALLQAHFFNTSGVFTTDFPSTPPHVFNYTGT PPKNLQTRNGTKVFRLAYNSTVQLVLQDTGIIAPENHPIHVHGFNFFAVGKGLGNYNPKTDPQKFNLVDPVERNTIGVPSGGWVAIRFRADNPGVWFMHC HLEVHTTWGLKMAFLVDNGKGP |
Full Sequence |
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Protein Sequence Length: 557 Download |
MYSSIRVLVV VAVLFPVFVD CTVRHYKFNV VMKNTTRLCS SKPIVSVNGK FPGPTLYARE 60 GDTVLVKVVN HVKYNVSIHW HGIRQLRTGW ADGPAYITQC PIQSGQSYVY NFTITGQRGT 120 LLWHAHILWL RSTVHGAIVI LPKRGVPYPF PKPHKEVVVV LAEWWKSDTE AVINEALKSG 180 LAPNVSDAHT INGHPGRVSG CPSQGGFSLP VESGKTYLLR LINAALNEEL FFKIAGHKLT 240 VVEVDATYVK PFKIDTVVIA PGQTTNVLVS ADQNSGKYMV AASPFMDAPV AVDNLTATAT 300 LHYSGTLDNT PTSLTTPPPQ NATSVANNFI DSLRSLNSKQ FPALVPRTID HNLYFTVGLG 360 INPCPTCKAG NGSRVVASIN NVTFTMPTTA LLQAHFFNTS GVFTTDFPST PPHVFNYTGT 420 PPKNLQTRNG TKVFRLAYNS TVQLVLQDTG IIAPENHPIH VHGFNFFAVG KGLGNYNPKT 480 DPQKFNLVDP VERNTIGVPS GGWVAIRFRA DNPGVWFMHC HLEVHTTWGL KMAFLVDNGK 540 GPNQSLLPPP SDLPKC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 2.0e-69 | 23 | 546 | 569 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 2.0e-86 | 23 | 534 | 540 | + oxidoreductase | ||
TIGR03388 | ascorbase | 1.0e-95 | 23 | 534 | 550 | + 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 | 21 | 556 | 539 | + 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_002308208.1 | 0 | 5 | 556 | 7 | 560 | laccase 1c [Populus trichocarpa] |
RefSeq | XP_002308209.1 | 0 | 8 | 556 | 2 | 550 | laccase 1d [Populus trichocarpa] |
RefSeq | XP_002322961.1 | 0 | 2 | 556 | 3 | 557 | laccase 1a [Populus trichocarpa] |
RefSeq | XP_002322962.1 | 0 | 2 | 556 | 3 | 557 | laccase 1b [Populus trichocarpa] |
RefSeq | XP_002533894.1 | 0 | 1 | 556 | 1 | 556 | 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 | 23 | 534 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asq_A | 0 | 23 | 534 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_B | 0 | 23 | 534 | 3 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |