| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_002_01054.3 |
| Family | CE10 |
| Protein Properties | Length: 355 Molecular Weight: 40210.9 Isoelectric Point: 10.2033 |
| Chromosome | Chromosome/Scaffold: 2 Start: 7910063 End: 7916224 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 193 | 339 | 1e-36 |
| QVHRSIVYGDQPRNRLDLYLPVNFDGPKPVVAFVTGGAWIIGYKAWGSLLGRRLAERDVIVACIDYRNFPQGTISDMVQDVSQGITYVCNNIADYGGDPN RIYLVGQSAGAHIASCVLVEQAIKESSKGDNISWSVSQIKAYFGISG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 355 Download |
| MIQVFSRRIH HTKQNQIINS QIFLKRTLIQ SNNQYQFHIL SVSKMQSQPF SSSSFSTKKD 60 EIKPESKPTM ASKRLEQEEE QQQQLTKPIL SKDHSTSFSK NLKNQQRRRK VTNNGSSSGT 120 SASRFLSRQQ SFRRDVEHAA AETFLLTRLS FTLLRYLGVG YRWITKFIAL TCYAMLLMPG 180 FLQVAYYYFF SKQVHRSIVY GDQPRNRLDL YLPVNFDGPK PVVAFVTGGA WIIGYKAWGS 240 LLGRRLAERD VIVACIDYRN FPQGTISDMV QDVSQGITYV CNNIADYGGD PNRIYLVGQS 300 AGAHIASCVL VEQAIKESSK GDNISWSVSQ IKAYFGISGG YNILNLVDHF HGRA* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 2.0e-8 | 208 | 321 | 128 | + 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 | 1.0e-9 | 228 | 311 | 85 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| pfam00135 | COesterase | 6.0e-10 | 210 | 311 | 125 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 1.0e-11 | 208 | 307 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 6.0e-21 | 198 | 306 | 111 | + Esterase/lipase [Lipid metabolism] | ||
| 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 |
| GenBank | ABD96862.1 | 0 | 105 | 354 | 43 | 288 | hypothetical protein [Cleome spinosa] |
| RefSeq | NP_186890.2 | 0 | 105 | 354 | 38 | 283 | unknown protein [Arabidopsis thaliana] |
| RefSeq | NP_197090.2 | 0 | 93 | 354 | 30 | 288 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
| RefSeq | XP_002264962.1 | 0 | 128 | 354 | 52 | 278 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002277990.1 | 0 | 86 | 354 | 51 | 319 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2hm7_A | 0.00000003 | 207 | 308 | 61 | 163 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1u4n_A | 0.00000003 | 207 | 308 | 61 | 163 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1qz3_A | 0.00000003 | 207 | 308 | 61 | 163 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
| PDB | 1evq_A | 0.00000003 | 207 | 308 | 61 | 163 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 2c7b_B | 0.0000003 | 207 | 309 | 61 | 163 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
