y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G093200.1 |
Family | CE10 |
Protein Properties | Length: 449 Molecular Weight: 49859.2 Isoelectric Point: 7.9922 |
Chromosome | Chromosome/Scaffold: 11 Start: 10125892 End: 10129626 |
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 | 101 | 438 | 0 |
PISLIQRRKSYGLLNMEAPRNDMRRSSFEGLDLRSDNNAYQGYAPSPQNCKKLPIMLQFHGGGWVSGSNDSVANDFFCRRIAKLCDVIVVAVGYRLAPEN KYPAAFEDGLKVLHWLGKQANLAECSKSMGSGARGVGAEFTKAEVQRHIVDAIGASVVEPWLAAHGDLSRCVLLGLSCGANIADYVARKAVEAGKLFDPV KVVAQVLMYPFFIGSVPTESEKKLANTYFYDKEMCTLAWKLFLPEEELSLDHPAGNPLILDRSPPLKLMPPTLTIVAEHDWMRDRAIAYSEALRNVNVVA PVLEYKDAVHEFANLDILLKTPQAQACAEDIVIWVKKY |
Full Sequence |
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Protein Sequence Length: 449 Download |
MPSLAVKLNS VFFKFLFKQR LQNRIQTPLN ESPNQYGITT RPEESVSASN PSFTDGVATK 60 DIHIDPFTAL SIRIFLPESS LSPPEQTGPK TKPKSSQQVY PISLIQRRKS YGLLNMEAPR 120 NDMRRSSFEG LDLRSDNNAY QGYAPSPQNC KKLPIMLQFH GGGWVSGSND SVANDFFCRR 180 IAKLCDVIVV AVGYRLAPEN KYPAAFEDGL KVLHWLGKQA NLAECSKSMG SGARGVGAEF 240 TKAEVQRHIV DAIGASVVEP WLAAHGDLSR CVLLGLSCGA NIADYVARKA VEAGKLFDPV 300 KVVAQVLMYP FFIGSVPTES EKKLANTYFY DKEMCTLAWK LFLPEEELSL DHPAGNPLIL 360 DRSPPLKLMP PTLTIVAEHD WMRDRAIAYS EALRNVNVVA PVLEYKDAVH EFANLDILLK 420 TPQAQACAED IVIWVKKYIS RRDNEFSY* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.0005 | 151 | 215 | 74 | + 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 | 2.0e-6 | 146 | 198 | 59 | + Carboxylesterase family. | ||
PRK10162 | PRK10162 | 2.0e-6 | 160 | 221 | 62 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 2.0e-38 | 96 | 432 | 339 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 9.0e-60 | 156 | 414 | 259 | + 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 | 1e-30 | 147 | 394 | 107 | 310 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 2zsh_A | 1e-30 | 147 | 394 | 107 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 9e-29 | 153 | 412 | 112 | 327 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 9e-29 | 153 | 412 | 112 | 327 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 9e-29 | 153 | 412 | 112 | 327 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES789976 | 350 | 106 | 449 | 0 |
DT546254 | 291 | 7 | 297 | 0 |
DT555368 | 278 | 77 | 354 | 0 |
EB438845 | 279 | 171 | 449 | 0 |
DT555368 | 27 | 356 | 382 | 0.0003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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