| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 419355 |
| Family | CE10 |
| Protein Properties | Length: 259 Molecular Weight: 29469.9 Isoelectric Point: 6.7113 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 44 | 123 | 8.2e-21 |
| SGLSARIFLPECEHGSKLPEFVYLHGGGFLVFTPKFQFFHYFCESMARNLKALVVSVDYRLAPEQRELKKVGNEKSHDQS | |||
| Full Sequence |
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| Protein Sequence Length: 259 Download |
| MALLHWIKAS LPGLPIDNKD DANYDDFAAT RQPLESIRTL YKISGLSARI FLPECEHGSK 60 LPEFVYLHGG GFLVFTPKFQ FFHYFCESMA RNLKALVVSV DYRLAPEQRE LKKVGNEKSH 120 DQSRGVVLVQ PFYGGMDRKD SEVEFANGEI LTMESSDLFW KLALPIGADR DHPYCNQPKF 180 LEENRVPREM APIFMAIGRK DCLYARQVEV ARRLQGANKH VQLVEYDDAA HAFYLGPPSS 240 ALDRFFVDLF GFMTMCCK* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 0.008 | 58 | 106 | 49 | + 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 | 0.0005 | 49 | 233 | 231 | + acetyl esterase; Provisional | ||
| COG2272 | PnbA | 0.0003 | 45 | 107 | 65 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 2.0e-20 | 29 | 245 | 260 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 6.0e-31 | 64 | 235 | 214 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2o7v_A | 6e-27 | 28 | 257 | 42 | 331 | A Chain A, The Crystal Structure Of A Hyperthermoactive Exopolygalacturonase From Thermotoga Maritima |
| PDB | 2o7r_A | 6e-27 | 28 | 257 | 42 | 331 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
| PDB | 3ed1_F | 8e-17 | 51 | 239 | 102 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
| PDB | 3ed1_E | 8e-17 | 51 | 239 | 102 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
| PDB | 3ed1_D | 8e-17 | 51 | 239 | 102 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
| Hydropathy |
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