| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.010G132200.3 |
| Family | CE10 |
| Protein Properties | Length: 438 Molecular Weight: 48863.9 Isoelectric Point: 7.0103 |
| Chromosome | Chromosome/Scaffold: 10 Start: 14689697 End: 14696887 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 138 | 385 | 0 |
| VLRSIVYGDQPRNRLDLYLPKNTDGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIMVACIDYRNYPQGTMSNMVEDASGGISFVCNKIAEYGGDPNR VYLMGQSAGGHIAACALVEQAIKEAGEGGSTTWSVLQIKTYFGLSGGYNLFNLVDYFHSRGLYRSIFLSIMEGEESLRRFSPEVIVQDPNLKKAVSLLPP IVLFHGTADYSIPADSSKSFAETLQSVGVRAESILYEGKTHTDLFLQD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 438 Download |
| MPSHILPVTN PNLHSSKQHS YLRIDPTTMP LKQDDPITST RLVSSPFEDE TIISVRPLLS 60 RTPSFADESI GQRQSLAREV DRAAPETFLL TRLGLKLLRY MGVGYRWIMR FLALGCYSLM 120 LFPGFIQVGY YYFFSGRVLR SIVYGDQPRN RLDLYLPKNT DGPKPVVAFV TGGAWIIGYK 180 AWGSLLGQQL SERDIMVACI DYRNYPQGTM SNMVEDASGG ISFVCNKIAE YGGDPNRVYL 240 MGQSAGGHIA ACALVEQAIK EAGEGGSTTW SVLQIKTYFG LSGGYNLFNL VDYFHSRGLY 300 RSIFLSIMEG EESLRRFSPE VIVQDPNLKK AVSLLPPIVL FHGTADYSIP ADSSKSFAET 360 LQSVGVRAES ILYEGKTHTD LFLQDPMRGG NDRMFEDLVS IIHSDDREAQ AKDEVAPPRR 420 RLVPEFMLQL AHRVSPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 4.0e-8 | 152 | 247 | 109 | + 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 | 8.0e-9 | 154 | 378 | 241 | + Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism] | ||
| COG2272 | PnbA | 1.0e-9 | 152 | 251 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 5.0e-11 | 172 | 378 | 226 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0657 | Aes | 5.0e-24 | 142 | 378 | 244 | + 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 |
| RefSeq | NP_173937.2 | 0 | 1 | 437 | 1 | 476 | esterase-related [Arabidopsis thaliana] |
| RefSeq | XP_002264962.1 | 0 | 72 | 437 | 52 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002277990.1 | 0 | 5 | 437 | 5 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315969.1 | 0 | 1 | 437 | 1 | 517 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514516.1 | 0 | 2 | 437 | 4 | 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 | 2c7b_B | 0.0000000000006 | 151 | 378 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2c7b_A | 0.0000000000006 | 151 | 378 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2hm7_A | 0.000000000004 | 151 | 378 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1evq_A | 0.000000000005 | 151 | 378 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1u4n_A | 0.00000000002 | 151 | 378 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
