| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.007G074300.1 |
| Family | CE10 |
| Protein Properties | Length: 444 Molecular Weight: 49218.2 Isoelectric Point: 7.7912 |
| Chromosome | Chromosome/Scaffold: 07 Start: 5265220 End: 5267956 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 110 | 433 | 0 |
| NIGARTNDSRRSSLEGSKLRSDNNVYRGYSPLPQNCRRLPIMLQFHGGGWVSGSNDSVANDIFCRRIAKLCDVIIVAVGYRLAPENKYPAAFEDGLKVLY WLAKQANLAECSKSMGSGALGVGAEFTKTQVQRHLVDAFGASMVEPWLAAHGDPSRCVLLGVSCGANIADYVARKAVEAGRLLDPVKVVAQVLMYPFFIG NVPTRSEINLANSYFYDKPMCLLAWKLFLPEEEFRLDHPAANPLVPDRGPPLKFMPPTLTVVAEHDWMRDRAIAYSEALRKVNVDAPVLEYKDAVHEFAT LDMLLNTPQAQACAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 444 Download |
| MPSIAVKLYS VFFKFLLKHR LQNRIQTHVD ESSNQYGVTT RPEESVSAAN PSFTDGIATK 60 DIHIDPSTAL SVRIFLPESS LSPPEPKSKP GSSQQDESDS LNHRRNSYPN IGARTNDSRR 120 SSLEGSKLRS DNNVYRGYSP LPQNCRRLPI MLQFHGGGWV SGSNDSVAND IFCRRIAKLC 180 DVIIVAVGYR LAPENKYPAA FEDGLKVLYW LAKQANLAEC SKSMGSGALG VGAEFTKTQV 240 QRHLVDAFGA SMVEPWLAAH GDPSRCVLLG VSCGANIADY VARKAVEAGR LLDPVKVVAQ 300 VLMYPFFIGN VPTRSEINLA NSYFYDKPMC LLAWKLFLPE EEFRLDHPAA NPLVPDRGPP 360 LKFMPPTLTV VAEHDWMRDR AIAYSEALRK VNVDAPVLEY KDAVHEFATL DMLLNTPQAQ 420 ACAEDIAIWV KKYISLRGHE FSY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 0.0001 | 133 | 275 | 152 | + 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 | 1.0e-5 | 155 | 216 | 62 | + acetyl esterase; Provisional | ||
| pfam00135 | COesterase | 7.0e-6 | 133 | 193 | 67 | + Carboxylesterase family. | ||
| COG0657 | Aes | 3.0e-37 | 130 | 427 | 299 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-61 | 151 | 408 | 258 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAS99713.1 | 0 | 1 | 443 | 1 | 428 | At3g27320 [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 443 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002267088.1 | 0 | 1 | 443 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002267130.1 | 0 | 1 | 443 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 443 | 1 | 472 | conserved hypothetical protein [Ricinus communis] |
| 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 | 1e-32 | 142 | 410 | 107 | 331 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 2zsh_A | 1e-32 | 142 | 410 | 107 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 3e-30 | 148 | 427 | 112 | 344 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 3e-30 | 148 | 427 | 112 | 344 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 3e-30 | 148 | 427 | 112 | 344 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| ES789976 | 356 | 104 | 444 | 0 |
| DT546254 | 286 | 7 | 292 | 0 |
| JK515504 | 268 | 177 | 444 | 0 |
| EB438845 | 279 | 166 | 444 | 0 |
| GO362523 | 304 | 136 | 434 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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