| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_002_01054.2 |
| Family | CE10 |
| Protein Properties | Length: 467 Molecular Weight: 52553.1 Isoelectric Point: 9.8618 |
| Chromosome | Chromosome/Scaffold: 2 Start: 7910063 End: 7916066 |
| Description | prenylcysteine methylesterase |
| 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 | 237 | 433 | 3.8e-29 |
| PQGTISDMVQDVSQGITYVCNNIADYGGDPNRIYLVGQSAGAHIASCVLVEQAIKESSKGDNISWSVSQIKAYFGISGGYNILNLVDHFHGRGLYRSIFL SIMEGTESLPRFSPEVLVQDPSTKTAVSLLPRIVLLHGTSDYSIPSEASETFADALQKVGARVELKLYKGKTHTDLFLQDPLRGGKDEVLEDILSII | |||
| Full Sequence |
|---|
| Protein Sequence Length: 467 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 WIIGNFPQGT 240 ISDMVQDVSQ GITYVCNNIA DYGGDPNRIY LVGQSAGAHI ASCVLVEQAI KESSKGDNIS 300 WSVSQIKAYF GISGGYNILN LVDHFHGRGL YRSIFLSIME GTESLPRFSP EVLVQDPSTK 360 TAVSLLPRIV LLHGTSDYSI PSEASETFAD ALQKVGARVE LKLYKGKTHT DLFLQDPLRG 420 GKDEVLEDIL SIIQAGETIA KDWEAPPIKR LVPEFMLQLA RKISPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 0.0001 | 208 | 296 | 125 | + 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. | ||
| COG1506 | DAP2 | 1.0e-5 | 210 | 409 | 238 | + Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism] | ||
| pfam00135 | COesterase | 7.0e-6 | 225 | 286 | 62 | + Carboxylesterase family. | ||
| pfam07859 | Abhydrolase_3 | 8.0e-7 | 254 | 409 | 165 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0657 | Aes | 7.0e-19 | 198 | 409 | 249 | + Esterase/lipase [Lipid metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0006508 | proteolysis |
| GO:0008152 | metabolic process |
| GO:0008236 | serine-type peptidase activity |
| 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 | 466 | 43 | 427 | hypothetical protein [Cleome spinosa] |
| RefSeq | NP_197090.2 | 0 | 93 | 466 | 30 | 427 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
| RefSeq | XP_002264962.1 | 0 | 128 | 466 | 52 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002277990.1 | 0 | 86 | 466 | 51 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002514516.1 | 0 | 128 | 466 | 80 | 445 | 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 | 2hm7_A | 0.000004 | 207 | 409 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1evq_A | 0.000005 | 207 | 409 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1u4n_A | 0.00001 | 207 | 409 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1qz3_A | 0.00001 | 207 | 409 | 61 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
| PDB | 1thg_A | 0.001 | 238 | 296 | 180 | 238 | A Chain A, 1.8 Angstroms Refined Structure Of The Lipase From Geotrichum Candidum |
