| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra032997 |
| Family | CE10 |
| Protein Properties | Length: 454 Molecular Weight: 49539.2 Isoelectric Point: 7.7893 |
| Chromosome | Chromosome/Scaffold: 02 Start: 22005182 End: 22007290 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 124 | 443 | 0 |
| SEARRSSYAHTTTASASSSSEEVYRGYAPSSSGKCRKLPVMLQFHGGGWVSGSNDSVANDFFCRRMAKHCDVIVLAVGYRLAPENRYPAACEDGFKVLQW LGKQANLAECNKSMGGGLRRGGGGGEVSKHVVDAFGASLVEPWLASHADPSRCVLLGVSCGANIADYVSRKAIEAGQNLDPVKVVAQVLMYPFFIGTVPT QSEIKQANSYFYDKPMCILAWKLFLPEEEFSLDHPAANPLVPDRGPPLKFMPPTLTIVAEHDWMRDRAIAYSEELRKVNVDAPVLEYKDAVHEFATLDML LRTPQAQACAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 454 Download |
| MPSVGVKLYS VFFKFLLKHR LQNRIQSEDS SSSSSSDPFG VTTRPEESVS PPNPLFTDGV 60 ATKDIHIDPL TSLSVRIFLP ESALSPASGS HSGKSRSFNS LAGSDLLLRR NSHGSSNSLS 120 SHKSEARRSS YAHTTTASAS SSSEEVYRGY APSSSGKCRK LPVMLQFHGG GWVSGSNDSV 180 ANDFFCRRMA KHCDVIVLAV GYRLAPENRY PAACEDGFKV LQWLGKQANL AECNKSMGGG 240 LRRGGGGGEV SKHVVDAFGA SLVEPWLASH ADPSRCVLLG VSCGANIADY VSRKAIEAGQ 300 NLDPVKVVAQ VLMYPFFIGT VPTQSEIKQA NSYFYDKPMC ILAWKLFLPE EEFSLDHPAA 360 NPLVPDRGPP LKFMPPTLTI VAEHDWMRDR AIAYSEELRK VNVDAPVLEY KDAVHEFATL 420 DMLLRTPQAQ ACAEDIAIWV KKYISLRGHE FSY* |
| 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-5 | 150 | 206 | 57 | + 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 | 5.0e-6 | 150 | 206 | 60 | + Carboxylesterase family. | ||
| PRK10162 | PRK10162 | 3.0e-7 | 168 | 236 | 69 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 3.0e-36 | 147 | 437 | 292 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-62 | 164 | 418 | 255 | + 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 | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAS99713.1 | 0 | 1 | 453 | 1 | 428 | At3g27320 [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 453 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | NP_189367.1 | 0 | 1 | 453 | 1 | 460 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002267088.1 | 0 | 1 | 453 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 453 | 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 | 2zsi_A | 3e-29 | 161 | 420 | 113 | 331 | A Chain A, Crystal Structure Of Soybean Beta-Amylase Complexed With Maltose |
| PDB | 2zsh_A | 3e-29 | 161 | 420 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 2e-27 | 161 | 420 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 2e-27 | 161 | 420 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 2e-27 | 161 | 420 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| ES789976 | 315 | 146 | 454 | 0 |
| EB438845 | 279 | 179 | 454 | 0 |
| JK515504 | 267 | 190 | 454 | 0 |
| DR937200 | 272 | 184 | 454 | 0 |
| DR937200 | 25 | 173 | 193 | 2.8 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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