y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra011010 |
Family | CE10 |
Protein Properties | Length: 461 Molecular Weight: 50698.8 Isoelectric Point: 7.2697 |
Chromosome | Chromosome/Scaffold: 08 Start: 17577556 End: 17580072 |
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 | 165 | 411 | 0 |
RRSIVYGDQPRNRLDLYLPKNSNGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGSISDMVKDASCGISYICNHIAEYGGDPNRI YLMGQSAGAHIAACTLVDQVVKESGEGDSVSWSSSQINAYFGLSGGYNLLSLVDHFHSRGLYRSIFLSIMEGEESLSQFSPELVVQNPNLKHIIARLPPI ILFHGTADYSIPSDASKSFAETLQRLGGKAEVILYEGKTHTDLFLQD |
Full Sequence |
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Protein Sequence Length: 461 Download |
MPSQILPFSY LPPPKSPPLA KQAMYKPLIY DDYPSTTTTT VKPLLSRAST FNASALATNG 60 GGGLTAWYHN KRRRSNSDNN CLSALPDRTN GTDGGDNGQQ TIAQEVTHAA AETFLLTRLC 120 LKLLSYLGVG YRWITRFMAL GCYAFLLMPG FVQVGYYYFF SPYVRRSIVY GDQPRNRLDL 180 YLPKNSNGPK PVVAFVTGGA WIIGYKAWGS LLGQQLSERD IIVACIDYRN FPQGSISDMV 240 KDASCGISYI CNHIAEYGGD PNRIYLMGQS AGAHIAACTL VDQVVKESGE GDSVSWSSSQ 300 INAYFGLSGG YNLLSLVDHF HSRGLYRSIF LSIMEGEESL SQFSPELVVQ NPNLKHIIAR 360 LPPIILFHGT ADYSIPSDAS KSFAETLQRL GGKAEVILYE GKTHTDLFLQ DPMRGGVDEM 420 FEDIVSVVLG GDSEVVGKSV DRRRLVPEFM LKLAHWVSPF * 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 7.0e-8 | 178 | 273 | 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. | ||
pfam00135 | COesterase | 2.0e-8 | 180 | 277 | 123 | + Carboxylesterase family. | ||
pfam07859 | Abhydrolase_3 | 6.0e-10 | 198 | 404 | 213 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG2272 | PnbA | 4.0e-10 | 178 | 277 | 115 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 3.0e-22 | 165 | 404 | 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 | AAG50528.1 | 0 | 1 | 460 | 1 | 472 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
RefSeq | NP_173937.2 | 0 | 1 | 460 | 1 | 476 | esterase-related [Arabidopsis thaliana] |
RefSeq | XP_002277990.1 | 0 | 41 | 460 | 51 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315969.1 | 0 | 1 | 460 | 1 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514516.1 | 0 | 7 | 460 | 21 | 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 | 0.00000000001 | 177 | 404 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.00000000002 | 177 | 404 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1u4n_A | 0.00000000007 | 177 | 404 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1qz3_A | 0.00000000007 | 177 | 404 | 61 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 2c7b_B | 0.0000000002 | 177 | 404 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |