y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.031590.1 |
Family | CE10 |
Protein Properties | Length: 428 Molecular Weight: 47795.8 Isoelectric Point: 7.2703 |
Chromosome | Chromosome/Scaffold: 00429 Start: 603018 End: 609874 |
Description | prenylcysteine methylesterase |
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 | 127 | 374 | 0 |
QVRRDIIYGTQPRNSLDLYLPTNTDKKKPVVIFVSGGAWIIGNKAWGALLGLQLAERDVIVASIDYRNFPQGTISDMVKDVSQGISFVCKNIADYGGDLD RIFLMGQSAGAHISVCALLDQAIKEARKGESVDWSVSQIKAYFGLSGGYNLWKLVDHFDSRGLYRSVFLSIMEGEESLSQFSPEIRIQDPSVSDVVSSLP PFVLFHGTGDYSIPFDASETFVETLRKAGAQADLFLYEGKTHTDLFLQ |
Full Sequence |
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Protein Sequence Length: 428 Download |
MAAPADRLRP VVKFSGQGIR FDDDDSTQTR PLLSRMLTYP IGIFHHQLRR RLGVGKPQVP 60 RRQQSFSRDF GHAAAETFLI TRLSFTLLRS LGVGYRWVVR LTALAVYAIL LMPGFLQVMY 120 DYYFSSQVRR DIIYGTQPRN SLDLYLPTNT DKKKPVVIFV SGGAWIIGNK AWGALLGLQL 180 AERDVIVASI DYRNFPQGTI SDMVKDVSQG ISFVCKNIAD YGGDLDRIFL MGQSAGAHIS 240 VCALLDQAIK EARKGESVDW SVSQIKAYFG LSGGYNLWKL VDHFDSRGLY RSVFLSIMEG 300 EESLSQFSPE IRIQDPSVSD VVSSLPPFVL FHGTGDYSIP FDASETFVET LRKAGAQADL 360 FLYEGKTHTD LFLQDPFRGG NYELFDQIVA ILHADDEEAL AKDSMAPPKP RLVPEVLIRL 420 ARMVSPF* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 1.0e-9 | 142 | 245 | 115 | + 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. | ||
pfam07859 | Abhydrolase_3 | 2.0e-10 | 157 | 368 | 220 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
pfam00135 | COesterase | 2.0e-12 | 144 | 245 | 118 | + Carboxylesterase family. | ||
COG2272 | PnbA | 2.0e-13 | 141 | 245 | 119 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 2.0e-19 | 129 | 368 | 247 | + Esterase/lipase [Lipid metabolism] |
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 | ABD96862.1 | 0 | 46 | 427 | 43 | 427 | hypothetical protein [Cleome spinosa] |
RefSeq | NP_197090.2 | 0 | 48 | 427 | 44 | 427 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
RefSeq | XP_002264962.1 | 0 | 60 | 427 | 50 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329262.1 | 0 | 49 | 427 | 3 | 377 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514516.1 | 0 | 11 | 427 | 45 | 445 | catalytic, putative [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 | 2hm7_A | 0.0000000009 | 144 | 368 | 64 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.000000001 | 144 | 368 | 64 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1u4n_A | 0.000000006 | 144 | 368 | 64 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1qz3_A | 0.000000006 | 144 | 368 | 64 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1thg_A | 0.00000003 | 131 | 237 | 93 | 220 | A Chain A, 1.8 Angstroms Refined Structure Of The Lipase From Geotrichum Candidum |