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Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi3g02300.1 |
Family | AA1 |
Protein Properties | Length: 590 Molecular Weight: 65385.4 Isoelectric Point: 6.3881 |
Chromosome | Chromosome/Scaffold: 3 Start: 1374854 End: 1377502 |
Description | laccase 7 |
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 | 23 | 571 | 0 |
AALVEHTFVVSQVKLNRLCNDTLMTVVNGQFPGPAIEITEGDSVAVHIVNMSPYGLTIHWHGVLVQMNCWADGAGMITQCPIQPNNNFTYRFDVVGQEGT LWWHAHVASLRASIHGALIIRPRASLYPFPRPDKEIPIIIGEWWEMDLVQLDRRLRNGLLFDMPSAATINGKPGDLYNCSGAIKETNILSIEHGKKYLLR IVNAVLNSEYYLKIAGHKFTVVGADANYVKPYTTDVIAIAPGQTVDALLVASDAHNPGGRYYMVAKANQPPKPAIQISRFISRATVQYNNNGPESKQDDE EADPVTAPEMPDEHDQITSFYFHGNLTSLQLPHPVPVNVDERLFFALDSGSFCDEGGSLPCVKTTNMTIHRFRNMVGTINNISFQLPATTPLLQAHYYNK VSSIDTLRDMPDRAPRMFYFSETIEPTSKATSVRRLPYNATVEIVFQSPLLGDTFANPMHLHGYNFFVLAQGFGMYRPERDVKRYNLVDPPVRNTVQVPI FGWAAVRFVANNPGVWFLHCHYGHHSSSGMATTFLVENGPTLDMSLPPP |
Full Sequence |
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Protein Sequence Length: 590 Download |
MAAAASMVFF LAVALAAASN SDAALVEHTF VVSQVKLNRL CNDTLMTVVN GQFPGPAIEI 60 TEGDSVAVHI VNMSPYGLTI HWHGVLVQMN CWADGAGMIT QCPIQPNNNF TYRFDVVGQE 120 GTLWWHAHVA SLRASIHGAL IIRPRASLYP FPRPDKEIPI IIGEWWEMDL VQLDRRLRNG 180 LLFDMPSAAT INGKPGDLYN CSGAIKETNI LSIEHGKKYL LRIVNAVLNS EYYLKIAGHK 240 FTVVGADANY VKPYTTDVIA IAPGQTVDAL LVASDAHNPG GRYYMVAKAN QPPKPAIQIS 300 RFISRATVQY NNNGPESKQD DEEADPVTAP EMPDEHDQIT SFYFHGNLTS LQLPHPVPVN 360 VDERLFFALD SGSFCDEGGS LPCVKTTNMT IHRFRNMVGT INNISFQLPA TTPLLQAHYY 420 NKVSSIDTLR DMPDRAPRMF YFSETIEPTS KATSVRRLPY NATVEIVFQS PLLGDTFANP 480 MHLHGYNFFV LAQGFGMYRP ERDVKRYNLV DPPVRNTVQV PIFGWAAVRF VANNPGVWFL 540 HCHYGHHSSS GMATTFLVEN GPTLDMSLPP PPEDLPACSE NYNTRLAYE* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 8.0e-71 | 41 | 556 | 549 | + L-ascorbate oxidase | ||
TIGR03388 | ascorbase | 2.0e-79 | 41 | 556 | 560 | + 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 | 28 | 578 | 560 | + 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 | NP_001064399.1 | 0 | 27 | 575 | 42 | 599 | Os10g0346300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001068353.1 | 0 | 20 | 561 | 25 | 565 | Os11g0641500 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001130676.1 | 0 | 18 | 561 | 21 | 578 | hypothetical protein LOC100191779 [Zea mays] |
RefSeq | XP_002449982.1 | 0 | 23 | 561 | 29 | 581 | hypothetical protein SORBIDRAFT_05g026630 [Sorghum bicolor] |
RefSeq | XP_002457562.1 | 0 | 15 | 578 | 20 | 593 | hypothetical protein SORBIDRAFT_03g009410 [Sorghum bicolor] |
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 | 41 | 556 | 19 | 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 | 41 | 556 | 19 | 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 | 41 | 556 | 19 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1asp_A | 0 | 41 | 556 | 19 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |
PDB | 1aso_B | 0 | 41 | 556 | 19 | 521 | A Chain A, Structure And Activity Of A Flavonoid 3-O Glucosyltransferase Reveals The Basis For Plant Natural Product Modification |