| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.B03069.3 |
| Family | CE10 |
| Protein Properties | Length: 405 Molecular Weight: 43734.7 Isoelectric Point: 8.8626 |
| Chromosome | Chromosome/Scaffold: 2 Start: 55644831 End: 55650089 |
| Description | alpha/beta-Hydrolases superfamily protein |
| 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 |
| CE10 | 179 | 393 | 5.8e-40 |
| VRRGIVYGDLPRNRLDLYLPKNMDGPKPVVAFITGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQVTIGDMVKDASQGISFVCNHIAEYGGDPNR VYLMGQSAGAHIAACALLEQAIKECGEGESTSWSVSQIKAYFGLSGGYNLLELVDYFHSRGLYRSLFLGIMEGEQSLQRYSPDLVARDPNIRTAVSRLPP VILFHGTADYSIPSD | |||
| Full Sequence |
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| Protein Sequence Length: 405 Download |
| MPSPLLPITN PSSHHHASSL SSLASSPASA VFGSKNGGAG GGRGRGRDDD PIANLLISSP 60 FDDEKAASVR PLLSRTSSYA SAGVAPAAAA APSSGLYQQR RRRSASENSL SSMSDNGRHQ 120 PLGREVADAT STRLGWRLLK YLGVGYRWIT RFLALGCYSL LLMPGFVQVG YYYFFSSQVR 180 RGIVYGDLPR NRLDLYLPKN MDGPKPVVAF ITGGAWIIGY KAWGSLLGQQ LSERDIIVAC 240 IDYRNFPQVT IGDMVKDASQ GISFVCNHIA EYGGDPNRVY LMGQSAGAHI AACALLEQAI 300 KECGEGESTS WSVSQIKAYF GLSGGYNLLE LVDYFHSRGL YRSLFLGIME GEQSLQRYSP 360 DLVARDPNIR TAVSRLPPVI LFHGTADYSI PSDARFVFLP GCIV* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 4.0e-8 | 193 | 301 | 124 | + 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. | ||
| pfam07859 | Abhydrolase_3 | 3.0e-8 | 210 | 296 | 88 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| pfam00135 | COesterase | 6.0e-10 | 195 | 296 | 125 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 1.0e-10 | 193 | 296 | 119 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 2.0e-19 | 183 | 396 | 221 | + Esterase/lipase [Lipid metabolism] | ||
| Gene Ontology | |
|---|---|
| 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 |
| GenBank | AAG50528.1 | 0 | 49 | 398 | 30 | 395 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
| RefSeq | NP_173937.2 | 0 | 49 | 398 | 30 | 399 | esterase-related [Arabidopsis thaliana] |
| RefSeq | XP_002264962.1 | 0 | 118 | 398 | 52 | 337 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002277990.1 | 0 | 1 | 398 | 1 | 378 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002514516.1 | 0 | 2 | 394 | 4 | 361 | catalytic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1lzl_A | 0.000000004 | 189 | 297 | 63 | 172 | A Chain A, Bacterial Heroin Esterase |
| PDB | 1lzk_A | 0.000000004 | 189 | 297 | 63 | 172 | A Chain A, Bacterial Heroin Esterase Complex With Transition State Analog Dimethylarsenic Acid |
| PDB | 2c7b_B | 0.0000001 | 192 | 293 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2c7b_A | 0.0000001 | 192 | 293 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2hm7_A | 0.0000003 | 187 | 293 | 54 | 163 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DY280956 | 302 | 98 | 398 | 0 |
| FC901726 | 285 | 97 | 365 | 0 |
| DY277968 | 286 | 97 | 366 | 0 |
| DY288531 | 289 | 98 | 385 | 0 |
| DY277968 | 32 | 367 | 398 | 0.27 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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