Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_55939g0010 |
Family | CE10 |
Protein Properties | Length: 252 Molecular Weight: 28160.8 Isoelectric Point: 6.5952 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 2 | 250 | 0 |
PVCLYFHGGAFVMGSPAWLCCHTLCIRMATAAGAIFVSVNYRLSPKHRLPAAYDDCFTAISWLRSEATKSNNNDGRDGDPWFQSHGDFSRLFLVGDSSGG NIVNHLIVNCSDWNPLKIRGAVMVQPSFGGERRTQSEMESPEAFEQSDRRRMMALPEGADRDHPFSNPFAPSSDYPTLAEATLPPFLIVIGGRDMKRDWG KAYYENLVKHGKTAQLIVFEEEIHGFYAFKKDAESTGELMRHIGDFVRA |
Full Sequence |
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Protein Sequence Length: 252 Download |
MPVCLYFHGG AFVMGSPAWL CCHTLCIRMA TAAGAIFVSV NYRLSPKHRL PAAYDDCFTA 60 ISWLRSEATK SNNNDGRDGD PWFQSHGDFS RLFLVGDSSG GNIVNHLIVN CSDWNPLKIR 120 GAVMVQPSFG GERRTQSEME SPEAFEQSDR RRMMALPEGA DRDHPFSNPF APSSDYPTLA 180 EATLPPFLIV IGGRDMKRDW GKAYYENLVK HGKTAQLIVF EEEIHGFYAF KKDAESTGEL 240 MRHIGDFVRA SN |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00135 | COesterase | 9.0e-5 | 1 | 46 | 46 | + Carboxylesterase family. | ||
cd00312 | Esterase_lipase | 9.0e-6 | 1 | 46 | 46 | + 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. | ||
PRK10162 | PRK10162 | 1.0e-9 | 6 | 250 | 267 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 5.0e-36 | 2 | 251 | 256 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 1.0e-61 | 5 | 228 | 228 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
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 | ABK25184.1 | 0 | 1 | 251 | 74 | 326 | unknown [Picea sitchensis] |
GenBank | ABK25952.1 | 0 | 1 | 251 | 74 | 326 | unknown [Picea sitchensis] |
GenBank | ABK26127.1 | 0 | 1 | 251 | 86 | 338 | unknown [Picea sitchensis] |
GenBank | ABK26852.1 | 0 | 1 | 248 | 72 | 321 | unknown [Picea sitchensis] |
GenBank | ABK26900.1 | 0 | 3 | 251 | 74 | 324 | unknown [Picea sitchensis] |
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 | 8.99998e-41 | 1 | 250 | 113 | 350 | A Chain A, Crystal Structure Of A Family Gh-19 Chitinase From Rye Seeds |
PDB | 2zsh_A | 8.99998e-41 | 1 | 250 | 113 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 7e-40 | 1 | 251 | 112 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 7e-40 | 1 | 251 | 112 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 7e-40 | 1 | 251 | 112 | 350 | 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 |
EX394764 | 252 | 1 | 252 | 0 |
DR572901 | 252 | 1 | 252 | 0 |
ES249404 | 250 | 1 | 250 | 0 |
DR468657 | 252 | 1 | 252 | 0 |
ES257039 | 252 | 1 | 252 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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