| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna10342.1-v1.0-hybrid |
| Family | CE10 |
| Protein Properties | Length: 507 Molecular Weight: 56151.7 Isoelectric Point: 7.5183 |
| Chromosome | Chromosome/Scaffold: 6 Start: 32222844 End: 32226857 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 230 | 472 | 0 |
| VQRSIVYGDQPRNRLDLYFPKNTDGKKPVVVFVTGGAWIIGYKAWGSLLGMQLAERNIIVACIDYRNFPQGTISDMVEDASRGISYICNNIADYGGDPDR IYLMGQSAGAHISSCALLEQAIKESKKEEISWSVSQIKAYFGLSGGIMEGEESFHRFSPEVRVQDPGNKDAVSILPPITLFHGTADYSIPSDASKIFVDV LQRVGAQADLVLYDGKTHTDLFLQDPLRGGKDDLFDQLVAVIH | |||
| Full Sequence |
|---|
| Protein Sequence Length: 507 Download |
| MVTPADGSYF VPDSCPSPFS IPLRLTPPNS TKPPDFSHRA EISFWRLLHC LLPWPSITKM 60 VFCILISILS VFVVAHAFLI FIFLRFTTTS LSDSIVKKMK LESPTESTAS SLRQSASSAV 120 AEELMEMETK PLLTKVLSYP PAATASIGQR RRTKSSPATP RPSRQNSFSR DIGHAAKETY 180 LVTSLSFTLL QYLGVGYRWI TRLLALYCYA MLLMPGFLQV AYLYYFSSQV QRSIVYGDQP 240 RNRLDLYFPK NTDGKKPVVV FVTGGAWIIG YKAWGSLLGM QLAERNIIVA CIDYRNFPQG 300 TISDMVEDAS RGISYICNNI ADYGGDPDRI YLMGQSAGAH ISSCALLEQA IKESKKEEIS 360 WSVSQIKAYF GLSGGIMEGE ESFHRFSPEV RVQDPGNKDA VSILPPITLF HGTADYSIPS 420 DASKIFVDVL QRVGAQADLV LYDGKTHTDL FLQDPLRGGK DDLFDQLVAV IHADDKEALE 480 QDAVAPPRRR LVPEILLKLA GNISPF* |
| 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-9 | 244 | 347 | 118 | + 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. | ||
| pfam00135 | COesterase | 3.0e-10 | 244 | 347 | 127 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 2.0e-10 | 244 | 347 | 118 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-11 | 259 | 447 | 210 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0657 | Aes | 6.0e-24 | 234 | 447 | 235 | + 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 - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2hm7_A | 0.000000004 | 243 | 447 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1f6w_A | 0.000000005 | 226 | 365 | 65 | 231 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
| PDB | 1evq_A | 0.000000006 | 243 | 447 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 2bce_A | 0.000000009 | 235 | 365 | 74 | 231 | A Chain A, Cholesterol Esterase From Bos Taurus |
| PDB | 1thg_A | 0.00000001 | 244 | 339 | 108 | 220 | A Chain A, 1.8 Angstroms Refined Structure Of The Lipase From Geotrichum Candidum |
