| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.031590.2 |
| Family | CE10 |
| Protein Properties | Length: 403 Molecular Weight: 44285 Isoelectric Point: 5.2341 |
| Chromosome | Chromosome/Scaffold: 00429 Start: 603018 End: 609874 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 102 | 349 | 0 |
| QVRRDIIYGTQPRNSLDLYLPTNTDKKKPVVIFVSGGAWIIGNKAWGALLGLQLAERDVIVASIDYRNFPQGTISDMVKDVSQGISFVCKNIADYGGDLD RIFLMGQSAGAHISVCALLDQAIKEARKGESVDWSVSQIKAYFGLSGGYNLWKLVDHFDSRGLYRSVFLSIMEGEESLSQFSPEIRIQDPSVSDVVSSLP PFVLFHGTGDYSIPFDASETFVETLRKAGAQADLFLYEGKTHTDLFLQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 403 Download |
| MIPPRLALCF PGCSLIRLGF STTSCAAVSA SESPKCHGAS SLLVEILAMQ LPKPFSLLAS 60 ASLSFDLLGY RWVVRLTALA VYAILLMPGF LQVMYDYYFS SQVRRDIIYG TQPRNSLDLY 120 LPTNTDKKKP VVIFVSGGAW IIGNKAWGAL LGLQLAERDV IVASIDYRNF PQGTISDMVK 180 DVSQGISFVC KNIADYGGDL DRIFLMGQSA GAHISVCALL DQAIKEARKG ESVDWSVSQI 240 KAYFGLSGGY NLWKLVDHFD SRGLYRSVFL SIMEGEESLS QFSPEIRIQD PSVSDVVSSL 300 PPFVLFHGTG DYSIPFDASE TFVETLRKAG AQADLFLYEG KTHTDLFLQD PFRGGNYELF 360 DQIVAILHAD DEEALAKDSM APPKPRLVPE VLIRLARMVS PF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 8.0e-10 | 117 | 220 | 115 | + 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-10 | 132 | 343 | 220 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| pfam00135 | COesterase | 1.0e-12 | 119 | 220 | 118 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 6.0e-14 | 116 | 220 | 119 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 3.0e-20 | 104 | 343 | 247 | + 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 | 63 | 402 | 84 | 427 | hypothetical protein [Cleome spinosa] |
| RefSeq | NP_197090.2 | 0 | 63 | 402 | 84 | 427 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
| RefSeq | XP_002305961.1 | 0 | 68 | 402 | 44 | 379 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002329262.1 | 0 | 68 | 402 | 43 | 377 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002533641.1 | 0 | 68 | 402 | 95 | 429 | carboxylesterase, 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 | 0.000000001 | 119 | 343 | 64 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1evq_A | 0.000000001 | 119 | 343 | 64 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1u4n_A | 0.000000007 | 119 | 343 | 64 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1qz3_A | 0.000000007 | 119 | 343 | 64 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
| PDB | 1thg_A | 0.00000003 | 106 | 212 | 93 | 220 | A Chain A, 1.8 Angstroms Refined Structure Of The Lipase From Geotrichum Candidum |
