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Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10013285m |
Family | AA1 |
Protein Properties | Length: 513 Molecular Weight: 56222.6 Isoelectric Point: 9.3331 |
Chromosome | Chromosome/Scaffold: 2 Start: 8684736 End: 8687049 |
Description | laccase 16 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA1 | 1 | 499 | 0 |
MTNTTKLCSSKPIVTVNGQFPGPTIVAREDDTVLIKVVNHVKYNVSIHWHGIRQLRTGWADGPAYITQCPIQPGQNYIYNFTLTGQRGTLWWHAHILWLR ATVHGAIVILPKLGVTYPFPKPYKEKTIVLGEWWKSDVEQLINDASRIGTAPIASDAHTINGHSGPISNCPSQRGYNLPVRPGKTYMLRIINAALNEDLF FKIAGHELTVVEVDAVYTKPFKTDTVLIAPGQTTNVLLTANANAGSKYMVAATTFMDAPILFDNVTATATLHYIGNTTVPASKKTVLASLPPQNATWVAT RFTRSLRSLNSREYPARVPTTVEHSLLFTVGLGANPCRSCINGVRLVAGINNVTFTMPSTALLQAHFFNIPHVFTDDFPARPLNPYNYTAPVTQSVNAAT MKGTKLYRLPYNATVQVVLQNTAMVGRGLGDFDPEKDPKVFNLVDPVERNTVGVPAGGWTAIRFLADNPGVWFMHCHLEIHTSWGLKMAFVVDNGHGPD |
Full Sequence |
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Protein Sequence Length: 513 Download |
MTNTTKLCSS KPIVTVNGQF PGPTIVARED DTVLIKVVNH VKYNVSIHWH GIRQLRTGWA 60 DGPAYITQCP IQPGQNYIYN FTLTGQRGTL WWHAHILWLR ATVHGAIVIL PKLGVTYPFP 120 KPYKEKTIVL GEWWKSDVEQ LINDASRIGT APIASDAHTI NGHSGPISNC PSQRGYNLPV 180 RPGKTYMLRI INAALNEDLF FKIAGHELTV VEVDAVYTKP FKTDTVLIAP GQTTNVLLTA 240 NANAGSKYMV AATTFMDAPI LFDNVTATAT LHYIGNTTVP ASKKTVLASL PPQNATWVAT 300 RFTRSLRSLN SREYPARVPT TVEHSLLFTV GLGANPCRSC INGVRLVAGI NNVTFTMPST 360 ALLQAHFFNI PHVFTDDFPA RPLNPYNYTA PVTQSVNAAT MKGTKLYRLP YNATVQVVLQ 420 NTAMVGRGLG DFDPEKDPKV FNLVDPVERN TVGVPAGGWT AIRFLADNPG VWFMHCHLEI 480 HTSWGLKMAF VVDNGHGPDQ SLLPPPADLP KC* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 3.0e-67 | 8 | 502 | 549 | + L-ascorbate oxidase | ||
PLN02604 | PLN02604 | 9.0e-80 | 8 | 490 | 524 | + oxidoreductase | ||
TIGR03388 | ascorbase | 1.0e-93 | 8 | 490 | 529 | + 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 | 1 | 512 | 533 | + 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 | ABE66261.1 | 0 | 1 | 512 | 1 | 530 | laccase/diphenol oxidase [Arabidopsis thaliana] |
GenBank | ABK28766.1 | 0 | 1 | 512 | 1 | 530 | unknown [Arabidopsis thaliana] |
RefSeq | NP_200699.1 | 0 | 1 | 512 | 1 | 523 | LAC16 (laccase 16); laccase [Arabidopsis thaliana] |
Swiss-Prot | Q1PDH6 | 0 | 1 | 512 | 37 | 566 | LAC16_ARATH RecName: Full=Laccase-16; AltName: Full=Benzenediol:oxygen oxidoreductase 16; AltName: Full=Urishiol oxidase 16; AltName: Full=Diphenol oxidase 16; Flags: Precursor |
RefSeq | XP_002314124.1 | 0 | 1 | 512 | 34 | 556 | predicted protein [Populus trichocarpa] |
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 | 8 | 490 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asq_A | 0 | 8 | 490 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1asp_B | 0 | 8 | 490 | 19 | 521 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797675 | 500 | 36 | 513 | 0 |
EL453925 | 335 | 44 | 378 | 0 |
JG648618 | 295 | 1 | 295 | 0 |
EE260547 | 271 | 5 | 275 | 0 |
DY266116 | 339 | 1 | 336 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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