y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.018G028400.1 |
Family | CE10 |
Protein Properties | Length: 224 Molecular Weight: 24791.4 Isoelectric Point: 7.8438 |
Chromosome | Chromosome/Scaffold: 18 Start: 2252050 End: 2252969 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 43 | 136 | 1.4e-22 |
VTIDSSKKITARLSLPDTPASMIQLPVVVHFHGGCFCFCSTTWLGFNHFPGDLSVASQSIVLSVDYRLAPENRLPIGYDDCFSSLERLCNNASS |
Full Sequence |
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Protein Sequence Length: 224 Download |
MSIVAEIPGF LQVFSDGLVK RFAPGIVPAS SKSYSNGFKF KDVTIDSSKK ITARLSLPDT 60 PASMIQLPVV VHFHGGCFCF CSTTWLGFNH FPGDLSVASQ SIVLSVDYRL APENRLPIGY 120 DDCFSSLERL CNNASSDPWL IKQADLSPII SFWRWCWMKH NTPDVSAGEW SEFPAVVVSV 180 TGLDFLNERG VMHAQFLARK GVKEVKLATP SLQQQRSEFT RSH* 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.005 | 58 | 112 | 56 | + 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. | ||
COG0657 | Aes | 9.0e-13 | 50 | 150 | 101 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 6.0e-19 | 70 | 150 | 86 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002285083.1 | 0 | 1 | 149 | 1 | 148 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002285083.1 | 0.0000000009 | 165 | 222 | 235 | 309 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002285088.1 | 0 | 1 | 146 | 1 | 145 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324857.1 | 0 | 1 | 149 | 1 | 148 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002324857.1 | 3e-16 | 164 | 223 | 233 | 310 | predicted protein [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 | 2o7v_A | 0.00000000000004 | 41 | 147 | 56 | 161 | A Chain A, Crystal Structure Of The Pseudomonas Aeruginosa Murg:udp-glcnac Substrate Comp |
PDB | 2o7r_A | 0.00000000000004 | 41 | 147 | 56 | 161 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2c7b_B | 0.0000000001 | 41 | 134 | 49 | 138 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.0000000001 | 41 | 134 | 49 | 138 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 3zwq_B | 0.00000003 | 39 | 133 | 50 | 140 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GH271644 | 148 | 2 | 149 | 0 |
EE663615 | 149 | 1 | 149 | 0 |
GH271363 | 145 | 5 | 149 | 0 |
DR929728 | 149 | 1 | 149 | 0 |
DR929728 | 39 | 165 | 203 | 0.00008 |
Sequence Alignments (This image is cropped. Click for full image.) |
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