Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna09070.1-v1.0-hybrid |
Family | CE10 |
Protein Properties | Length: 269 Molecular Weight: 29521.8 Isoelectric Point: 5.3855 |
Chromosome | Chromosome/Scaffold: 2 Start: 20996503 End: 20997959 |
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 | 35 | 266 | 4.40008e-43 |
QTYKPNITETSPKLPLIVYYHGGAFCIASAAEPLYHNCLNMLVAGARAIAISVSYRLAPEHPLPIAYEDSWAALEYVFGGEELDEWVKDHVDLKRVFLVG YSVGANIAHHLALRVKKSNPDPKVKIVEEVDGGYMVFVCPSEKGGDDRLINPFINGSPSLEGLACGKVLVLVVGEDILRDRGRLYYDELVKSNRAGSKEL IETEGEDHVFHIFNPNEEKAKTLIKDLGSFIN |
Full Sequence |
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Protein Sequence Length: 269 Download |
MGSNEVLLDV SPYARVLKDG TIERLNGTQV VPAGQTYKPN ITETSPKLPL IVYYHGGAFC 60 IASAAEPLYH NCLNMLVAGA RAIAISVSYR LAPEHPLPIA YEDSWAALEY VFGGEELDEW 120 VKDHVDLKRV FLVGYSVGAN IAHHLALRVK KSNPDPKVKI VEEVDGGYMV FVCPSEKGGD 180 DRLINPFING SPSLEGLACG KVLVLVVGED ILRDRGRLYY DELVKSNRAG SKELIETEGE 240 DHVFHIFNPN EEKAKTLIKD LGSFINQK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG2272 | PnbA | 3.0e-7 | 47 | 142 | 113 | + Carboxylesterase type B [Lipid metabolism] | ||
cd00312 | Esterase_lipase | 2.0e-9 | 37 | 148 | 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. | ||
pfam00135 | COesterase | 1.0e-9 | 37 | 147 | 133 | + Carboxylesterase family. | ||
COG0657 | Aes | 4.0e-22 | 11 | 266 | 282 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-43 | 51 | 246 | 221 | + 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 | 2e-27 | 48 | 268 | 113 | 351 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |
PDB | 2zsh_A | 2e-27 | 48 | 268 | 113 | 351 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 1e-23 | 48 | 266 | 112 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 1e-23 | 48 | 266 | 112 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 1e-23 | 48 | 266 | 112 | 348 | 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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