| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi1g34707.1 |
| Family | CE10 |
| Protein Properties | Length: 468 Molecular Weight: 51715.7 Isoelectric Point: 8.5233 |
| Chromosome | Chromosome/Scaffold: 1 Start: 30312782 End: 30317399 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 167 | 432 | 0 |
| QVHRSVVYGEQPRNRLDLYIPTGTTESKPVVAFITGGAWIIGYKGWGALLGRRLAERGILVACIDYRNFPQGTIGDMVEDASQGISFICNNIASYGGDPE RIYLVGQSAGAHIAACTLLNQAIKECGEGDTSTWSIAQLKAYFGISGGYNLLNLVDHFHRRGLYRSIFLSIMEGEESLKKFSPQVMVKESASRSALPLLP HIFLFHGTSDCSIPCAESQAFLDALQQHGAKADLFLYEGKTHTDLFLQDPLRGGRDKMLEEIVAAI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 468 Download |
| MEVELPARAA SQPGKARETP PPSPVAAVAS LAEDAPLLPG GAGAGVRRRP VSEQFRQRSA 60 SLRRDVGRAA AETFLLSRLA LILLRYLGYP PIPFSLLLAL RSALLLTVGA IEYVNRMEWF 120 RSDPWVKSDR FRIGYRWIRQ FLALCCYALL LMPGFIQVLY YYFFSNQVHR SVVYGEQPRN 180 RLDLYIPTGT TESKPVVAFI TGGAWIIGYK GWGALLGRRL AERGILVACI DYRNFPQGTI 240 GDMVEDASQG ISFICNNIAS YGGDPERIYL VGQSAGAHIA ACTLLNQAIK ECGEGDTSTW 300 SIAQLKAYFG ISGGYNLLNL VDHFHRRGLY RSIFLSIMEG EESLKKFSPQ VMVKESASRS 360 ALPLLPHIFL FHGTSDCSIP CAESQAFLDA LQQHGAKADL FLYEGKTHTD LFLQDPLRGG 420 RDKMLEEIVA AIHNDDPGES AQHLPVPVAR RLVPEIMLIL ARRVSPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07859 | Abhydrolase_3 | 3.0e-9 | 199 | 285 | 88 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| cd00312 | Esterase_lipase | 5.0e-10 | 182 | 290 | 123 | + 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 | 4.0e-10 | 182 | 285 | 118 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam00135 | COesterase | 3.0e-10 | 182 | 285 | 116 | + Carboxylesterase family. | ||
| COG0657 | Aes | 7.0e-26 | 172 | 432 | 269 | + 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 | ACG46361.1 | 0 | 1 | 467 | 1 | 418 | carboxylesterase-like protein [Zea mays] |
| GenBank | EAZ02309.1 | 0 | 1 | 467 | 1 | 425 | hypothetical protein OsI_24410 [Oryza sativa Indica Group] |
| RefSeq | NP_001058531.1 | 0 | 1 | 467 | 1 | 425 | Os06g0708100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001132117.1 | 0 | 29 | 467 | 3 | 404 | hypothetical protein LOC100193534 [Zea mays] |
| RefSeq | XP_002264962.1 | 0 | 58 | 467 | 52 | 417 | 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 | 0.000000003 | 181 | 283 | 61 | 164 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1u4n_A | 0.000000004 | 181 | 283 | 61 | 164 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1qz3_A | 0.000000004 | 181 | 283 | 61 | 164 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
| PDB | 1evq_A | 0.000000004 | 181 | 283 | 61 | 164 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1f6w_A | 0.00000004 | 168 | 284 | 69 | 205 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
