| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 123940 |
| Family | CE10 |
| Protein Properties | Length: 405 Molecular Weight: 43325.4 Isoelectric Point: 6.3444 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 121 | 399 | 0 |
| SKQEHVKLPVIVQFHGGAFVSGSKDSSSNDVFCRRIAKACKCIVIAVGYRLAPDNKFPAPRDDGIFTLKWLAKQGNLAAFPATAVSHGIIESFGQMPADP WISAHVDYSRCALMGIGAGGTIAEQVSQACVSLKLELEPLKVVSQVLIYPLLGGSTPLPSEISLADAYFLDREMLALAWSWFLPEEHLAVASSIDPRSSS RSSILSKMPSTLVISAELDMLRDRAAAYVQALKMVSVDASFLTYRNAVHGFATIDCFLDTKLAQACVEDIAIWFAKHVK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 405 Download |
| MRDGRAVSNR AAQGSNTRVP PNASFVDGVA TKDCIIDPAT GVAIRIFLPH HCLGVSDAAG 60 SKGFGWLPRD HTAPGDEESL RSSLELSDGS SVGSSNGNSD NEKLLALEEA LKFSGGYFPA 120 SKQEHVKLPV IVQFHGGAFV SGSKDSSSND VFCRRIAKAC KCIVIAVGYR LAPDNKFPAP 180 RDDGIFTLKW LAKQGNLAAF PATAVSHGII ESFGQMPADP WISAHVDYSR CALMGIGAGG 240 TIAEQVSQAC VSLKLELEPL KVVSQVLIYP LLGGSTPLPS EISLADAYFL DREMLALAWS 300 WFLPEEHLAV ASSIDPRSSS RSSILSKMPS TLVISAELDM LRDRAAAYVQ ALKMVSVDAS 360 FLTYRNAVHG FATIDCFLDT KLAQACVEDI AIWFAKHVKC DYWG* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 8.0e-5 | 117 | 200 | 93 | + 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 | 3.0e-6 | 117 | 243 | 143 | + Carboxylesterase family. | ||
| PRK10162 | PRK10162 | 5.0e-8 | 117 | 180 | 64 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 6.0e-28 | 117 | 399 | 284 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-49 | 131 | 372 | 242 | + 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 | 2zsi_A | 1e-28 | 128 | 371 | 113 | 328 | A Chain A, Crystal Structure Of Orotidine 5'-monophosphate Decarboxylase From Sulfolobus Solfataricus Complexed With Inhibitor Bmp |
| PDB | 2zsh_A | 1e-28 | 128 | 371 | 113 | 328 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3aim_D | 6e-28 | 117 | 379 | 82 | 303 | A Chain A, R267e Mutant Of A Hsl-Like Carboxylesterase From Sulfolobus Tokodaii |
| PDB | 3aim_C | 6e-28 | 117 | 379 | 82 | 303 | A Chain A, R267e Mutant Of A Hsl-Like Carboxylesterase From Sulfolobus Tokodaii |
| PDB | 3aim_B | 6e-28 | 117 | 379 | 82 | 303 | A Chain A, R267e Mutant Of A Hsl-Like Carboxylesterase From Sulfolobus Tokodaii |
| Hydropathy |
|---|
 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
| Phylogeny |
|---|
 |