y
Basic Information | |
---|---|
Species | Arabidopsis thaliana |
Cazyme ID | AT3G27320.2 |
Family | CE10 |
Protein Properties | Length: 429 Molecular Weight: 47182.7 Isoelectric Point: 7.0271 |
Chromosome | Chromosome/Scaffold: 3 Start: 10090065 End: 10092791 |
Description | CXE carboxylesterase, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CE10 | 72 | 418 | 0 |
SVRIFLPESALTPLEPSTSACVYSESRRNSYGYTTGSSSPEAGSSDVYRGYAPSSSGGNSRKLPVMLQFHGGGWVSGSNDSVANDFFCRRMAKHCDIIVL AVGYRLAPENRYPAACEDGFKVLKWLGKQANLAECNKSMGNSRRPGGEVKKSEVNKHIVDAFGASLVEPWLANHADPSRCVLLGVSCGANIADYVARKAI EVGQNLDPVKVVAQVLMYPFFIGSVPTQSEIKQANSYFYDKPMCILAWKLFLPEEEFSLDHQAANPLVPGRSPPLKFMPPTLTIVAEHDWMRDRAIAYSE ELRKVNVDAPVLEYKDAVHEFATLDMLLRTPQAQACAEDIAIWAKKY |
Full Sequence |
---|
Protein Sequence Length: 429 Download |
MPSVGVKLYS VFFKFLLKHR LQNRIQSSGD ESSSDPFGVT TRPEESVAAP NPLFTDGVAT 60 KDIHIDPLTS LSVRIFLPES ALTPLEPSTS ACVYSESRRN SYGYTTGSSS PEAGSSDVYR 120 GYAPSSSGGN SRKLPVMLQF HGGGWVSGSN DSVANDFFCR RMAKHCDIIV LAVGYRLAPE 180 NRYPAACEDG FKVLKWLGKQ ANLAECNKSM GNSRRPGGEV KKSEVNKHIV DAFGASLVEP 240 WLANHADPSR CVLLGVSCGA NIADYVARKA IEVGQNLDPV KVVAQVLMYP FFIGSVPTQS 300 EIKQANSYFY DKPMCILAWK LFLPEEEFSL DHQAANPLVP GRSPPLKFMP PTLTIVAEHD 360 WMRDRAIAYS EELRKVNVDA PVLEYKDAVH EFATLDMLLR TPQAQACAED IAIWAKKYIS 420 LRGHEFSY* 480 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.0005 | 122 | 179 | 58 | + 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 | 2.0e-5 | 122 | 179 | 61 | + Carboxylesterase family. | ||
PRK10162 | PRK10162 | 8.0e-7 | 141 | 209 | 69 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 3.0e-36 | 113 | 412 | 301 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 5.0e-60 | 137 | 393 | 257 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
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 | AAS99713.1 | 0 | 1 | 428 | 1 | 428 | At3g27320 [Arabidopsis thaliana] |
RefSeq | NP_001030781.1 | 0 | 1 | 428 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
RefSeq | NP_189367.1 | 0 | 1 | 428 | 1 | 460 | hydrolase [Arabidopsis thaliana] |
RefSeq | XP_002267130.1 | 0 | 1 | 428 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002526925.1 | 0 | 1 | 428 | 1 | 472 | conserved hypothetical protein [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2o7v_A | 3e-30 | 35 | 379 | 27 | 295 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2o7r_A | 3e-30 | 35 | 379 | 27 | 295 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsi_A | 7e-28 | 134 | 395 | 113 | 331 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsh_A | 7e-28 | 134 | 395 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 2e-26 | 134 | 395 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
ES789976 | 349 | 87 | 429 | 0 |
EB438845 | 279 | 152 | 429 | 0 |
GO362523 | 304 | 120 | 419 | 0 |
DR937200 | 273 | 157 | 429 | 0 |
DR937200 | 25 | 146 | 166 | 2.6 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|
![]() |