| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.001G268100.1 |
| Family | CE10 |
| Protein Properties | Length: 449 Molecular Weight: 49677.6 Isoelectric Point: 8.0108 |
| Chromosome | Chromosome/Scaffold: 01 Start: 54506444 End: 54510402 |
| 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 | 107 | 438 | 0 |
| RRSSYAPSNVGAPRNDPRRSSLEGLNLRSDNNVYRGYSPSPQNCRKLPIMLQFHGGGWVSGSNESVANDYFCRRIAKLCDVIVIAVGYRLAPENKYPAAF EDGLKVLNWLAKQANLSECSKSMGSGARGVGSEFTKAEVQRHIVDTFGASVVEPWLAAHGDPSRCVLLGVSCGANIVDYVARKAVEAGKRLDPVKVVAQV LMYPFFIGNVPTQSEIKLANSYFYDKAMCLLAWKLFLPKEEFSLDHPAANPLISDRGPPLKFMPPTLTVVAEHDWMRDRAIAYSETLRKVNVDAPVLEYK DAVHEFATLDMLLKTPQAQACAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 449 Download |
| MPSVALKLYS VFFKFLLKHR LQNLIQNAID ESSNPYGVTT RPEESVSASN PSFTDGVATK 60 DIHIDPFTAL SIRIFLPDSS LSPPEQPDLK PNLRSSGNDD PNSHNHRRSS YAPSNVGAPR 120 NDPRRSSLEG LNLRSDNNVY RGYSPSPQNC RKLPIMLQFH GGGWVSGSNE SVANDYFCRR 180 IAKLCDVIVI AVGYRLAPEN KYPAAFEDGL KVLNWLAKQA NLSECSKSMG SGARGVGSEF 240 TKAEVQRHIV DTFGASVVEP WLAAHGDPSR CVLLGVSCGA NIVDYVARKA VEAGKRLDPV 300 KVVAQVLMYP FFIGNVPTQS EIKLANSYFY DKAMCLLAWK LFLPKEEFSL DHPAANPLIS 360 DRGPPLKFMP PTLTVVAEHD WMRDRAIAYS ETLRKVNVDA PVLEYKDAVH EFATLDMLLK 420 TPQAQACAED IAIWVKKYIS TRGHEFSY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10162 | PRK10162 | 5.0e-6 | 141 | 221 | 81 | + acetyl esterase; Provisional | ||
| pfam00135 | COesterase | 1.0e-6 | 138 | 285 | 166 | + Carboxylesterase family. | ||
| cd00312 | Esterase_lipase | 7.0e-7 | 138 | 280 | 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. | ||
| COG0657 | Aes | 2.0e-39 | 135 | 432 | 299 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-61 | 156 | 413 | 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 | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABB89022.1 | 0 | 1 | 434 | 1 | 450 | CXE carboxylesterase [Actinidia deliciosa] |
| RefSeq | NP_001030781.1 | 0 | 1 | 448 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002267088.1 | 0 | 1 | 448 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002267130.1 | 0 | 1 | 448 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 448 | 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 | 2e-31 | 147 | 415 | 107 | 331 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
| PDB | 2zsh_A | 2e-31 | 147 | 415 | 107 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 1e-27 | 153 | 415 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 1e-27 | 153 | 415 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 1e-27 | 153 | 415 | 112 | 330 | 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 |
| DT555368 | 279 | 77 | 355 | 0 |
| ES789976 | 376 | 86 | 449 | 0 |
| JK515504 | 268 | 182 | 449 | 0 |
| DT546254 | 288 | 7 | 294 | 0 |
| DT555368 | 27 | 356 | 382 | 0.000001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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