| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_10277324g0010 |
| Family | CE10 |
| Protein Properties | Length: 107 Molecular Weight: 11336.8 Isoelectric Point: 4.9689 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 8 | 90 | 3.9e-26 |
| LGQELVERNVIVACIDYRNFPQGTISDMVKDASQGISFVCNNIAEYGGDPNRIYLVGQSAGAHIAACALVDQAIKEAGTERTG | |||
| Full Sequence |
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| Protein Sequence Length: 107 Download |
| YKAWGALLGQ ELVERNVIVA CIDYRNFPQG TISDMVKDAS QGISFVCNNI AEYGGDPNRI 60 YLVGQSAGAH IAACALVDQA IKEAGTERTG LTWSVSQIKA FVGISGG |
| 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-6 | 16 | 69 | 63 | + 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. | ||
| COG2272 | PnbA | 9.0e-7 | 9 | 73 | 79 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 7.0e-7 | 11 | 73 | 64 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| pfam00135 | COesterase | 9.0e-9 | 12 | 86 | 99 | + Carboxylesterase family. | ||
| COG0657 | Aes | 4.0e-12 | 12 | 73 | 62 | + Esterase/lipase [Lipid metabolism] | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_002264962.1 | 0 | 1 | 107 | 159 | 264 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002277990.1 | 0 | 1 | 107 | 200 | 305 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315969.1 | 0 | 1 | 107 | 259 | 364 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002329262.1 | 0 | 1 | 107 | 119 | 224 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514516.1 | 0 | 1 | 107 | 187 | 292 | 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 | 1jmy_A | 0.0000007 | 9 | 85 | 127 | 221 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
| PDB | 1f6w_A | 0.000002 | 9 | 85 | 127 | 221 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
| PDB | 1thg_A | 0.000004 | 17 | 77 | 157 | 228 | A Chain A, 1.8 Angstroms Refined Structure Of The Lipase From Geotrichum Candidum |
| PDB | 2bce_A | 0.000006 | 9 | 101 | 127 | 235 | A Chain A, Cholesterol Esterase From Bos Taurus |
| PDB | 2c7b_B | 0.000007 | 16 | 95 | 104 | 184 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
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| Hit | Length | Start | End | EValue |
| DV994832 | 107 | 1 | 107 | 0 |
| GE476752 | 107 | 1 | 107 | 0 |
| DV994928 | 107 | 1 | 107 | 0 |
| GE479256 | 107 | 1 | 107 | 0 |
| CO481830 | 107 | 1 | 107 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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