| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 871194 |
| Family | AA1 |
| Protein Properties | Length: 570 Molecular Weight: 63804.9 Isoelectric Point: 8.1442 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA1 | 29 | 561 | 0 |
| ATTRFYQFKVQTIRLTRLCQTNEIVTVNGKFPGPAISAQEDDRIVVKVINMTPYNTTIHWHGIKQKLSCWYDGPSYITQCPIQSGQSFTYNFKVAQQKGT FLWHAHFSWLRATVYGPLIVYPKASVPYPFKKPFNEHTILLGEYWLKNVVELEQHVLESGGPPPPADAFTINGQPGPNYNCSSKDVYEIQIVPRKTYLLR LINAGINMETFFTIANHRLTIVEVDGEYTKPYTTERVMLVPGQTMNILVTADQAVGRYSMAMGPYESAKNVEFQNTSAIANFQYIGALPNSVTVPAKLPI FNDNIAVKTVMDGLRSLNAVDVPRNIDAHLFITIGINVNKCNSENPNNKCQGPRKGRLAASMNNISFVEPKISILEAYYKQLEGYFTLDFPTTPEKAYDF VNGAPNDIANDTQAANGTRAIVFEYGSRIQIIFQNTGTLTTENHPIHLHGHSFYVIGYGTGNYDQQTAQFNLEDPPYMNTIGVPVGGWAAIRFVANNPGL WLLHCHFDIHQTWGMSTMFIVKNGKKVQESLPH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 570 Download |
| MTDSAAPCLF RLSFFLFTLQ VMNVGRVSAT TRFYQFKVQT IRLTRLCQTN EIVTVNGKFP 60 GPAISAQEDD RIVVKVINMT PYNTTIHWHG IKQKLSCWYD GPSYITQCPI QSGQSFTYNF 120 KVAQQKGTFL WHAHFSWLRA TVYGPLIVYP KASVPYPFKK PFNEHTILLG EYWLKNVVEL 180 EQHVLESGGP PPPADAFTIN GQPGPNYNCS SKDVYEIQIV PRKTYLLRLI NAGINMETFF 240 TIANHRLTIV EVDGEYTKPY TTERVMLVPG QTMNILVTAD QAVGRYSMAM GPYESAKNVE 300 FQNTSAIANF QYIGALPNSV TVPAKLPIFN DNIAVKTVMD GLRSLNAVDV PRNIDAHLFI 360 TIGINVNKCN SENPNNKCQG PRKGRLAASM NNISFVEPKI SILEAYYKQL EGYFTLDFPT 420 TPEKAYDFVN GAPNDIANDT QAANGTRAIV FEYGSRIQII FQNTGTLTTE NHPIHLHGHS 480 FYVIGYGTGN YDQQTAQFNL EDPPYMNTIG VPVGGWAAIR FVANNPGLWL LHCHFDIHQT 540 WGMSTMFIVK NGKKVQESLP HPPADLPKC* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02191 | PLN02191 | 6.0e-68 | 14 | 548 | 580 | + L-ascorbate oxidase | ||
| TIGR03388 | ascorbase | 5.0e-82 | 31 | 547 | 564 | + 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. | ||
| PLN02604 | PLN02604 | 1.0e-82 | 11 | 547 | 577 | + oxidoreductase | ||
| TIGR03389 | laccase | 0 | 29 | 569 | 547 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN75876.1 | 0 | 30 | 569 | 32 | 571 | hypothetical protein [Vitis vinifera] |
| RefSeq | NP_182180.1 | 0 | 1 | 569 | 1 | 569 | LAC6 (laccase 6); laccase [Arabidopsis thaliana] |
| RefSeq | XP_002264410.1 | 0 | 30 | 569 | 32 | 571 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002320207.1 | 0 | 41 | 569 | 1 | 529 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523314.1 | 0 | 30 | 569 | 33 | 572 | laccase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 32 | 547 | 4 | 521 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asq_A | 0 | 32 | 547 | 4 | 521 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asp_B | 0 | 32 | 547 | 4 | 521 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1asp_A | 0 | 32 | 547 | 4 | 521 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 1aso_B | 0 | 32 | 547 | 4 | 521 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
