| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.013G079100.1 |
| Family | CE10 |
| Protein Properties | Length: 463 Molecular Weight: 50752.8 Isoelectric Point: 6.5856 |
| Chromosome | Chromosome/Scaffold: 13 Start: 10561752 End: 10567191 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 162 | 411 | 0 |
| QVRRSIIYGEKPRNRLDLYLPKTSQGTKPVVAFITGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGTISDMVEDASQGISFICNNISEYGGDPN RIYLMGQSAGAHIAACTLVNQAIKETGEGDSVSWSVSQIKAYLGLSGGYNLFNLIEHFHTRGLYRSIFLSIMEGEDSLHQFSPEVLVQDSDVKPAVSLLP PVILFHGTADYSIPADSSQNFADTLRRVGGKAESILYYGKTHTDLFLQDP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 463 Download |
| MPSPILPISS HPSSSASAAT TVVKAKIDAD PSATILISSK FDPEKAIPIT PVLPRASSYN 60 STSNVNNNIV SFANNHQQRF LRTSSDSSLA LLADETPRQS ISREVGHVAA ETFYLSGLCL 120 KLLSYLGVGY RWITRFLALG CYAMLLMPGF IQVAFYYFFS RQVRRSIIYG EKPRNRLDLY 180 LPKTSQGTKP VVAFITGGAW IIGYKAWGSL LGQQLSERDI IVACIDYRNF PQGTISDMVE 240 DASQGISFIC NNISEYGGDP NRIYLMGQSA GAHIAACTLV NQAIKETGEG DSVSWSVSQI 300 KAYLGLSGGY NLFNLIEHFH TRGLYRSIFL SIMEGEDSLH QFSPEVLVQD SDVKPAVSLL 360 PPVILFHGTA DYSIPADSSQ NFADTLRRVG GKAESILYYG KTHTDLFLQD PMRGGRDEMF 420 EDVVAIIHGE DEAALAKDAV APPRRRLVPE FMLKLAHDVS PF* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 3.0e-8 | 177 | 272 | 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. | ||
| pfam00135 | COesterase | 1.0e-9 | 179 | 284 | 142 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 9.0e-10 | 177 | 276 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-10 | 194 | 403 | 215 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0657 | Aes | 3.0e-23 | 164 | 403 | 247 | + 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 | AAG50528.1 | 0 | 1 | 462 | 1 | 472 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
| RefSeq | NP_173937.2 | 0 | 1 | 462 | 1 | 476 | esterase-related [Arabidopsis thaliana] |
| RefSeq | XP_002277990.1 | 0 | 1 | 462 | 1 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315969.1 | 0 | 1 | 462 | 1 | 517 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514516.1 | 0 | 2 | 462 | 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 | 0.00000000004 | 176 | 403 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2c7b_A | 0.00000000004 | 176 | 403 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
| PDB | 2hm7_A | 0.000000005 | 176 | 394 | 61 | 273 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
| PDB | 1evq_A | 0.000000006 | 176 | 394 | 61 | 273 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
| PDB | 1u4n_A | 0.000000009 | 176 | 394 | 61 | 273 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
