| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10013549m |
| Family | CE10 |
| Protein Properties | Length: 446 Molecular Weight: 49316.3 Isoelectric Point: 8.1606 |
| Chromosome | Chromosome/Scaffold: 2 Start: 4681524 End: 4683405 |
| Description | carboxyesterase 16 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 100 | 435 | 0 |
| QPRSDRRHSHGSLNQNSPPNESRRNSYGCNIENLEPYGGYAPSPKRNSRKLPVMLQFHGGGWVSGSSDSAANDFFCRRIAKVCDVIVLAVGYRLAPDNRY PAAFEDGVKVLHWLGKQANLADCCKCVGNRRVNGVELKKLSVQGQIVDAFGASMVEPWLAAHADPSRCVLLGVSCGGNIADYVARKAVEAGKLLEPVKVV AQVLMYPFFIGNNPTQSEIKLANSYFYDKPVSVLAWKLFLPEKEFNFDHPAANPLAHNRTGPPLKLMPPTLTVVAEHDWMRDRAIAYAEELRKVNVDSPV LEYKDAVHEFATLDMLLKTPQAQACAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 446 Download |
| MPSVAVKLYS VFFKLLLKHR LQNLISISAD GLSDSFGVST RSDESVAAAN PSFTDGVATK 60 DIHIDPMTSL TVRIFLPESA LSPSEPDSLK LHHRDNYQHQ PRSDRRHSHG SLNQNSPPNE 120 SRRNSYGCNI ENLEPYGGYA PSPKRNSRKL PVMLQFHGGG WVSGSSDSAA NDFFCRRIAK 180 VCDVIVLAVG YRLAPDNRYP AAFEDGVKVL HWLGKQANLA DCCKCVGNRR VNGVELKKLS 240 VQGQIVDAFG ASMVEPWLAA HADPSRCVLL GVSCGGNIAD YVARKAVEAG KLLEPVKVVA 300 QVLMYPFFIG NNPTQSEIKL ANSYFYDKPV SVLAWKLFLP EKEFNFDHPA ANPLAHNRTG 360 PPLKLMPPTL TVVAEHDWMR DRAIAYAEEL RKVNVDSPVL EYKDAVHEFA TLDMLLKTPQ 420 AQACAEDIAI WVKKYISIRG HEFSY* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10162 | PRK10162 | 9.0e-7 | 113 | 218 | 111 | + acetyl esterase; Provisional | ||
| cd00312 | Esterase_lipase | 5.0e-7 | 139 | 212 | 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 | 6.0e-8 | 139 | 220 | 97 | + Carboxylesterase family. | ||
| COG0657 | Aes | 8.0e-35 | 135 | 429 | 295 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-61 | 153 | 410 | 258 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAB87770.1 | 0 | 1 | 445 | 1 | 439 | putative protein [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 445 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | NP_189367.1 | 0 | 1 | 445 | 1 | 460 | hydrolase [Arabidopsis thaliana] |
| RefSeq | NP_568298.1 | 0 | 1 | 445 | 1 | 446 | AtCXE16 (Arabidopsis thaliana carboxyesterase 16); hydrolase |
| RefSeq | XP_002526925.1 | 0 | 1 | 445 | 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 | 3e-32 | 150 | 412 | 113 | 331 | A Chain A, The Crystal Structure Of Geotrichum Sp. M128 Xyloglucanase |
| PDB | 2zsh_A | 3e-32 | 150 | 412 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 5e-29 | 150 | 412 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 5e-29 | 150 | 412 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 5e-29 | 150 | 412 | 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 | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EX130706 | 271 | 178 | 446 | 0 |
| ES789976 | 357 | 105 | 446 | 0 |
| EB438845 | 280 | 168 | 446 | 0 |
| JK515504 | 268 | 179 | 446 | 0 |
| EV055706 | 230 | 177 | 404 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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