| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 29929.m004742 |
| Family | CE10 |
| Protein Properties | Length: 391 Molecular Weight: 43118.6 Isoelectric Point: 8.5247 |
| Chromosome | Chromosome/Scaffold: 29929 Start: 1397993 End: 1399850 |
| 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 | 55 | 382 | 0 |
| FTDGVATKDIHVDPFSSLSLRIFLPETALSSSSSSSLINTSPYGGYSPPPGKFHRKLPVMLQFHGGGFVSGSNESVANDVFCRRIAKLCDVIVIAVGYRL APESKYPAAFEDGVKVLNWLVKQAHLAACRRLGVQSGIFDSFGASMLEPWLAAHGDPGRCVLLGASSGANIADYVARKSVEAGKLLDPVKVVAQVLMYPF FIGSTPTGSEVKLANSYFYDKSMCKLAWKLFLPEDEFKLDHPAANPLLRGRQTPLKYMPSTLIVVADNDFMRDRAIAYSEELRKVNVDAPLLDYKDAVHE FASLDMLLQTPQAKACAEDISIWVKKYV | |||
| Full Sequence |
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| Protein Sequence Length: 391 Download |
| MPSVIVKLYS VFFKYQYRHL LQNISDQSAI TNNKPNPFGI TSRPHESIVS SNPSFTDGVA 60 TKDIHVDPFS SLSLRIFLPE TALSSSSSSS LINTSPYGGY SPPPGKFHRK LPVMLQFHGG 120 GFVSGSNESV ANDVFCRRIA KLCDVIVIAV GYRLAPESKY PAAFEDGVKV LNWLVKQAHL 180 AACRRLGVQS GIFDSFGASM LEPWLAAHGD PGRCVLLGAS SGANIADYVA RKSVEAGKLL 240 DPVKVVAQVL MYPFFIGSTP TGSEVKLANS YFYDKSMCKL AWKLFLPEDE FKLDHPAANP 300 LLRGRQTPLK YMPSTLIVVA DNDFMRDRAI AYSEELRKVN VDAPLLDYKD AVHEFASLDM 360 LLQTPQAKAC AEDISIWVKK YVSLRGNEFS Y |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 1.0e-7 | 106 | 223 | 127 | + 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 | 9.0e-8 | 109 | 228 | 132 | + Carboxylesterase family. | ||
| PRK10162 | PRK10162 | 6.0e-8 | 118 | 217 | 108 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 1.0e-34 | 106 | 375 | 271 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-60 | 114 | 357 | 244 | + 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 - PDB Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2zsi_A | 5e-39 | 49 | 355 | 60 | 328 | A Chain A, The 1.6 A Structure Of Fe-superoxide Dismutase From The Thermophilic Cyanobacterium Thermosynechococcus Elongatus : Correlation Of Epr And Structural Characteristics |
| PDB | 2zsh_A | 5e-39 | 49 | 355 | 60 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 5e-34 | 49 | 338 | 52 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 5e-34 | 49 | 338 | 52 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 5e-34 | 49 | 338 | 52 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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