y
Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_014_00724.3 |
Family | CE1 |
Protein Properties | Length: 235 Molecular Weight: 26166.5 Isoelectric Point: 6.9195 |
Chromosome | Chromosome/Scaffold: 14 Start: 4234106 End: 4237148 |
Description | S-formylglutathione hydrolase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE1 | 25 | 224 | 2.7003e-42 |
SPVLGCSMTFSVYFPPSPSPSSKFPVLYWLSGLSCTDENFIAKSGAQRAASREGVALIAPDTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWKNWRMYD YVVKELPKVLSENFEQLDTSRASISGHSMGGHGALTIYLKNLDKYKSVSAFAPVSNPINCPWGQKAFSNYLGDNKSDWEEYDATCLILKHNNVLARILID |
Full Sequence |
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Protein Sequence Length: 235 Download |
MDLKPNEISS SKMFEGYNKR YKHYSPVLGC SMTFSVYFPP SPSPSSKFPV LYWLSGLSCT 60 DENFIAKSGA QRAASREGVA LIAPDTSPRG LNVEGEADSW DFGVGAGFYL NATQEKWKNW 120 RMYDYVVKEL PKVLSENFEQ LDTSRASISG HSMGGHGALT IYLKNLDKYK SVSAFAPVSN 180 PINCPWGQKA FSNYLGDNKS DWEEYDATCL ILKHNNVLAR ILIDQVNSQL LFQV* 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00756 | Esterase | 2.0e-41 | 25 | 225 | 204 | + Putative esterase. This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family. | ||
COG0627 | COG0627 | 9.0e-56 | 8 | 214 | 224 | + Predicted esterase [General function prediction only] | ||
TIGR02821 | fghA_ester_D | 3.0e-99 | 8 | 225 | 219 | + S-formylglutathione hydrolase. This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well [Cellular processes, Detoxification]. | ||
PLN02442 | PLN02442 | 1.0e-161 | 1 | 225 | 225 | + S-formylglutathione hydrolase |
Gene Ontology | |
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GO Term | Description |
GO:0004091 | carboxylesterase activity |
GO:0006508 | proteolysis |
GO:0008236 | serine-type peptidase activity |
GO:0016023 | cytoplasmic membrane-bounded vesicle |
GO:0018738 | S-formylglutathione 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 | ACJ11734.1 | 0 | 1 | 233 | 1 | 239 | S-formylglutathione hydrolase [Gossypium hirsutum] |
GenBank | ACU18661.1 | 0 | 1 | 225 | 1 | 225 | unknown [Glycine max] |
RefSeq | NP_181684.1 | 0 | 6 | 225 | 6 | 225 | SFGH (S-FORMYLGLUTATHIONE HYDROLASE); S-formylglutathione hydrolase/ hydrolase, acting on ester bonds [Arabidopsis thaliana] |
RefSeq | XP_002284489.1 | 0 | 1 | 225 | 1 | 225 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002308013.1 | 0 | 1 | 225 | 1 | 225 | esterase d, s-formylglutathione hydrolase [Populus trichocarpa] |
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 | 3fcx_B | 0 | 1 | 225 | 1 | 222 | A Chain A, Crystal Structure Of Human Esterase D |
PDB | 3fcx_A | 0 | 1 | 225 | 1 | 222 | A Chain A, Crystal Structure Of Human Esterase D |
PDB | 3s8y_A | 0 | 8 | 225 | 7 | 221 | A Chain A, Bromide Soaked Structure Of An Esterase From The Oil-Degrading Bacterium Oleispira Antarctica |
PDB | 3i6y_B | 0 | 8 | 225 | 7 | 221 | A Chain A, Structure Of An Esterase From The Oil-Degrading Bacterium Oleispira Antarctica |
PDB | 3i6y_A | 0 | 8 | 225 | 7 | 221 | A Chain A, Structure Of An Esterase From The Oil-Degrading Bacterium Oleispira Antarctica |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT758794 | 225 | 1 | 225 | 0 |
DT756717 | 225 | 1 | 225 | 0 |
DT759710 | 225 | 1 | 225 | 0 |
DR944783 | 224 | 2 | 225 | 0 |
JG618514 | 222 | 4 | 225 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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