Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna17534.1-v1.0-hybrid |
Family | CE10 |
Protein Properties | Length: 327 Molecular Weight: 35906.5 Isoelectric Point: 5.0776 |
Chromosome | Chromosome/Scaffold: 2 Start: 11916980 End: 11917960 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 39 | 318 | 1.4013e-45 |
DPQTGVSSKDITISHNPLVSARLYLPAQNQSQKQLPIFVYFHAGGFFCSSAFSFYHHRYLNRLVSEAQVIAVSVEYRLAPESPLPAAYEDSWLSLQWVAS HSLHEDDTCNNKEPWLADFGDFDRVYIGGDSAGGNISHNIAIKAGVESLNGGVKILGAILSHSGFWGSTPIGSEPRGEDFEKSLSYLVLKFSFPCADGGL DNPMINPMAPGAPSLAGLECSRLLVCVAGKDELRDRNLWYYASVKESGWKGEAELFEVEEGEHCFHIASDEVTENVKKMI |
Full Sequence |
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Protein Sequence Length: 327 Download |
MASTTKEIVS EIPNLIKHYK DGTVERLIAD PHVPPSLNDP QTGVSSKDIT ISHNPLVSAR 60 LYLPAQNQSQ KQLPIFVYFH AGGFFCSSAF SFYHHRYLNR LVSEAQVIAV SVEYRLAPES 120 PLPAAYEDSW LSLQWVASHS LHEDDTCNNK EPWLADFGDF DRVYIGGDSA GGNISHNIAI 180 KAGVESLNGG VKILGAILSH SGFWGSTPIG SEPRGEDFEK SLSYLVLKFS FPCADGGLDN 240 PMINPMAPGA PSLAGLECSR LLVCVAGKDE LRDRNLWYYA SVKESGWKGE AELFEVEEGE 300 HCFHIASDEV TENVKKMIKR MADFLV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.0007 | 61 | 172 | 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. | ||
PRK10162 | PRK10162 | 0.0003 | 94 | 175 | 83 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 4.0e-19 | 36 | 325 | 298 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-37 | 94 | 305 | 215 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
Gene Ontology | |
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GO Term | Description |
GO:0008152 | metabolic process |
GO:0016787 | hydrolase activity |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2zsi_A | 5e-34 | 21 | 305 | 45 | 330 | A Chain A, Crystal Structure Of A Beta-Galactosidase From Bacteroides Thetaiotaomicron |
PDB | 2zsh_A | 5e-34 | 21 | 305 | 45 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 2e-33 | 16 | 325 | 32 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 2e-33 | 16 | 325 | 32 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 2e-33 | 16 | 325 | 32 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
Sequence Alignments (This image is cropped. Click for full image.) |
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