| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi2g15577.1 |
| Family | CE10 |
| Protein Properties | Length: 399 Molecular Weight: 43802.3 Isoelectric Point: 9.1324 |
| Chromosome | Chromosome/Scaffold: 2 Start: 13846024 End: 13850468 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 103 | 340 | 0 |
| RSVVYGNQPRNRLDLYIPKDHSKPHPVVAFVTGGAWIIGYKAWGALLGRRLAERGIMVACIDYRNFPQGTIGDMVTDASEGIAFICESIASFGGDPNQIY LMGQSAGAHIAACSLLEQAVKESKGEEIYWSVTQIKGYFGLSGGYNVQNLVDHFHERGLYRSIFLSIMEGRRSLADFSPEIVAKKLSPEAIALLPQVVLF HGTGDYSIPSSASETFADVLKQAGAKARLQLYKGKTHT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 399 Download |
| MQPTTPVSAG RAGNSPKNLR RRGPSAPSIP SARWTRTTFR EDVGHAAAET YLVSRLAFIL 60 LRSLGVGYRW ICQLVALLIY AVLLMPGFIK VGQYYFFSSQ VLRSVVYGNQ PRNRLDLYIP 120 KDHSKPHPVV AFVTGGAWII GYKAWGALLG RRLAERGIMV ACIDYRNFPQ GTIGDMVTDA 180 SEGIAFICES IASFGGDPNQ IYLMGQSAGA HIAACSLLEQ AVKESKGEEI YWSVTQIKGY 240 FGLSGGYNVQ NLVDHFHERG LYRSIFLSIM EGRRSLADFS PEIVAKKLSP EAIALLPQVV 300 LFHGTGDYSI PSSASETFAD VLKQAGAKAR LQLYKGKTHT DVFVQDPLRG GKDPLVEDVV 360 SIIQADDPAA REKYDSGPLP ERLVSEWQIM LARQISPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07859 | Abhydrolase_3 | 4.0e-8 | 135 | 339 | 215 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| cd00312 | Esterase_lipase | 2.0e-9 | 115 | 223 | 126 | + 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 | 6.0e-10 | 115 | 218 | 119 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 1.0e-10 | 115 | 227 | 127 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 3.0e-24 | 105 | 339 | 242 | + 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 | 15 | 398 | 41 | 427 | hypothetical protein [Cleome spinosa] |
| GenBank | EAY99150.1 | 0 | 2 | 398 | 71 | 458 | hypothetical protein OsI_21109 [Oryza sativa Indica Group] |
| GenBank | EEE55068.1 | 0 | 36 | 398 | 47 | 409 | hypothetical protein OsJ_02788 [Oryza sativa Japonica Group] |
| RefSeq | NP_001056406.1 | 0 | 1 | 398 | 1 | 414 | Os05g0577200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001132117.1 | 0 | 8 | 398 | 17 | 404 | hypothetical protein LOC100193534 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1u4n_A | 0.0000000006 | 114 | 339 | 61 | 282 | A Chain A, D-Hydantoinase (Dihydropyrimidinase) From Thermus Sp. In Space Group C2221 |
| PDB | 1qz3_A | 0.0000000006 | 114 | 339 | 61 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
| PDB | 2hm7_A | 0.0000000007 | 114 | 339 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1evq_A | 0.000000001 | 114 | 339 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 4e15_B | 0.000000003 | 107 | 342 | 63 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
