| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 488268 |
| Family | CE10 |
| Protein Properties | Length: 448 Molecular Weight: 49456.4 Isoelectric Point: 8.215 |
| Chromosome | Chromosome/Scaffold: 6 Start: 5776277 End: 5778510 |
| Description | carboxyesterase 16 |
| 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 |
| CE10 | 102 | 437 | 0 |
| SDRRHSYGPNHNSPAPAERNESRRNSYGCNNENLVPYGGYAPSAKRNSRKLPVMLQFHGGGWVSGSSDSAANDFFCRRIAKVCDVIVLAVGYRLAPENRY PAAFEDGVKVLNWLGKQANLAECCKSLGNRRVNGVEVKKLNVQGQIVDAFGASMVEPWLAAHADPSRCVLLGVSCGGNIADYVARKAVEAGKLLEPVKVV AQVLMYPFFIGNNPTQSEIKLANSYFYDKPVSVLAWKLFLPEKEFDFDHPAANPLAHNRSGPPLKLMPPTLTVVAEHDWMRDRAIAYSEELRKVNVDSPV LEYKDAVHEFATLDMLLKTPQAQACAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 448 Download |
| MPGVAVKLYS VFFKLLLKHR LQNLISISAA DGLSDSFGVS TRSDESVAAA NPSFTDGVAT 60 KDIHIDPMTS LTVRIFLPES ALSPPEPDSL RHKDHFHHQP RSDRRHSYGP NHNSPAPAER 120 NESRRNSYGC NNENLVPYGG YAPSAKRNSR KLPVMLQFHG GGWVSGSSDS AANDFFCRRI 180 AKVCDVIVLA VGYRLAPENR YPAAFEDGVK VLNWLGKQAN LAECCKSLGN RRVNGVEVKK 240 LNVQGQIVDA FGASMVEPWL AAHADPSRCV LLGVSCGGNI ADYVARKAVE AGKLLEPVKV 300 VAQVLMYPFF IGNNPTQSEI KLANSYFYDK PVSVLAWKLF LPEKEFDFDH PAANPLAHNR 360 SGPPLKLMPP TLTVVAEHDW MRDRAIAYSE ELRKVNVDSP VLEYKDAVHE FATLDMLLKT 420 PQAQACAEDI AIWVKKYISI RGHEFSY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 3.0e-6 | 141 | 214 | 83 | + Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. | ||
| pfam00135 | COesterase | 3.0e-7 | 141 | 197 | 60 | + Carboxylesterase family. | ||
| PRK10162 | PRK10162 | 3.0e-7 | 136 | 220 | 90 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 5.0e-35 | 109 | 431 | 323 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-61 | 155 | 412 | 258 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
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| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAB87770.1 | 0 | 1 | 447 | 1 | 439 | putative protein [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 447 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | NP_568298.1 | 0 | 1 | 447 | 1 | 446 | AtCXE16 (Arabidopsis thaliana carboxyesterase 16); hydrolase |
| RefSeq | XP_002267088.1 | 0 | 1 | 447 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 447 | 1 | 472 | conserved hypothetical protein [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2zsi_A | 1e-33 | 152 | 414 | 113 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 2zsh_A | 1e-33 | 152 | 414 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 7e-30 | 152 | 414 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 7e-30 | 152 | 414 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 7e-30 | 152 | 414 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| ES789976 | 361 | 104 | 448 | 0 |
| EX130706 | 271 | 180 | 448 | 0 |
| EB438845 | 280 | 170 | 448 | 0 |
| JK515504 | 268 | 181 | 448 | 0 |
| EV055706 | 230 | 179 | 406 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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