Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g038598m |
Family | AA1 |
Protein Properties | Length: 393 Molecular Weight: 43116.9 Isoelectric Point: 7.9126 |
Chromosome | Chromosome/Scaffold: 00014 Start: 73049 End: 74690 |
Description | laccase 17 |
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 | 379 | 0 |
EWFNADPEAIINQSLQTGNGPNVSEAYTFNGLPGPTYNCSAKDTYKLKVKPGKTYMLRLINTALNDELFFSIANHTLTVVEADAIYVKPFETNILVIAPG QTTNVLLKTNPNPPNASFFMLARPYFTGMGTFDNSTVAAILEYEAPSQDNSFRNRTLFKPSLPAINDTNFVANFSSKFRSLANAQFPANVPQTVDKRFFF TVSLGANPCPKNQTCQGPNGTKFAAAVNNVSFALPSTALLQSYFFAKSKGVYTADFPQFPLHPFNYTGTPPNNTFVSNGTKALDTSILGAESHPLHLHGY NVYVVGQGFGNFDPKNDPKKFNLIDPVERNTVGVPSGGWVAIRFLADNPGVWFMHCHFDVHLSWGLRMAWIVLDGELPN |
Full Sequence |
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Protein Sequence Length: 393 Download |
EWFNADPEAI INQSLQTGNG PNVSEAYTFN GLPGPTYNCS AKDTYKLKVK PGKTYMLRLI 60 NTALNDELFF SIANHTLTVV EADAIYVKPF ETNILVIAPG QTTNVLLKTN PNPPNASFFM 120 LARPYFTGMG TFDNSTVAAI LEYEAPSQDN SFRNRTLFKP SLPAINDTNF VANFSSKFRS 180 LANAQFPANV PQTVDKRFFF TVSLGANPCP KNQTCQGPNG TKFAAAVNNV SFALPSTALL 240 QSYFFAKSKG VYTADFPQFP LHPFNYTGTP PNNTFVSNGT KALDTSILGA ESHPLHLHGY 300 NVYVVGQGFG NFDPKNDPKK FNLIDPVERN TVGVPSGGWV AIRFLADNPG VWFMHCHFDV 360 HLSWGLRMAW IVLDGELPNQ KLPPPPSDLP KC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02191 | PLN02191 | 3.0e-38 | 47 | 382 | 359 | + L-ascorbate oxidase | ||
pfam00394 | Cu-oxidase | 7.0e-41 | 1 | 144 | 148 | + Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. | ||
PLN02604 | PLN02604 | 2.0e-43 | 6 | 379 | 397 | + oxidoreductase | ||
TIGR03388 | ascorbase | 9.0e-53 | 22 | 366 | 371 | + 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 | 392 | 406 | + 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_002299296.1 | 0 | 1 | 392 | 173 | 581 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300066.1 | 0 | 1 | 392 | 172 | 580 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002308164.1 | 0 | 1 | 392 | 175 | 580 | laccase 110b [Populus trichocarpa] |
RefSeq | XP_002313424.1 | 0 | 1 | 392 | 178 | 576 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531824.1 | 0 | 1 | 392 | 174 | 576 | 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 | 3e-32 | 22 | 382 | 181 | 536 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asq_A | 3e-32 | 22 | 382 | 181 | 536 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asp_B | 3e-32 | 22 | 382 | 181 | 536 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1asp_A | 3e-32 | 22 | 382 | 181 | 536 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1aso_B | 3e-32 | 22 | 382 | 181 | 536 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
JG213352 | 293 | 65 | 344 | 0 |
CV230599 | 265 | 142 | 393 | 0 |
FG609471 | 313 | 2 | 299 | 0 |
HO797675 | 410 | 1 | 393 | 0 |
FG609471 | 36 | 302 | 337 | 0.014 |
Sequence Alignments (This image is cropped. Click for full image.) |
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