y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.010G132200.4 |
Family | CE10 |
Protein Properties | Length: 385 Molecular Weight: 42694.8 Isoelectric Point: 8.9308 |
Chromosome | Chromosome/Scaffold: 10 Start: 14689727 End: 14696846 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 166 | 381 | 2.1e-37 |
VLRSIVYGDQPRNRLDLYLPKNTDGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIMVACIDYRNYPQGTMSNMVEDASGGISFVCNKIAEYGGDPNR VYLMGQSAGGHIAACALVEQAIKEAGEGGSTTWSVLQIKTYFGLSGGYNLFNLVDYFHSRGLYRSIFLSIMEGEESLRRFSPEVIVQDPNLKKAVSLLPP IVLFHGTADYSIPADS |
Full Sequence |
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Protein Sequence Length: 385 Download |
MPSHILPVTN PNLHSSKQHS YLRIDPTTMP LKQDDPITST RLVSSPFEDE TIISVRPLLS 60 RTPSFAGTTT TSSSASYQQR RRRVASENSL SSLSDESIGQ RQSLAREVDR AAPETFLLTR 120 LGLKLLRYMG VGYRWIMRFL ALGCYSLMLF PGFIQVGYYY FFSGRVLRSI VYGDQPRNRL 180 DLYLPKNTDG PKPVVAFVTG GAWIIGYKAW GSLLGQQLSE RDIMVACIDY RNYPQGTMSN 240 MVEDASGGIS FVCNKIAEYG GDPNRVYLMG QSAGGHIAAC ALVEQAIKEA GEGGSTTWSV 300 LQIKTYFGLS GGYNLFNLVD YFHSRGLYRS IFLSIMEGEE SLRRFSPEVI VQDPNLKKAV 360 SLLPPIVLFH GTADYSIPAD SRIQ* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07859 | Abhydrolase_3 | 5.0e-7 | 200 | 279 | 86 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
pfam00135 | COesterase | 3.0e-7 | 182 | 279 | 119 | + Carboxylesterase family. | ||
cd00312 | Esterase_lipase | 4.0e-8 | 180 | 275 | 109 | + 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. | ||
COG2272 | PnbA | 7.0e-10 | 180 | 279 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 2.0e-18 | 170 | 378 | 216 | + 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 | AAG50528.1 | 0 | 1 | 381 | 1 | 391 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
RefSeq | NP_173937.2 | 0 | 1 | 381 | 1 | 395 | esterase-related [Arabidopsis thaliana] |
RefSeq | XP_002277990.1 | 0 | 5 | 381 | 5 | 374 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315969.1 | 0 | 1 | 381 | 1 | 433 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514516.1 | 0 | 2 | 381 | 4 | 361 | 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 | 2c7b_B | 0.0000000006 | 179 | 280 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.0000000006 | 179 | 280 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 1lzl_A | 0.0000000009 | 162 | 284 | 46 | 172 | A Chain A, Bacterial Heroin Esterase |
PDB | 1lzk_A | 0.0000000009 | 162 | 284 | 46 | 172 | A Chain A, Bacterial Heroin Esterase Complex With Transition State Analog Dimethylarsenic Acid |
PDB | 2hm7_A | 0.000000004 | 179 | 280 | 61 | 163 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |