y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_5588g0010 |
Family | CE10 |
Protein Properties | Length: 355 Molecular Weight: 39067.5 Isoelectric Point: 6.3184 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 88 | 347 | 0 |
QQQTEKRRLPLIVYFHGGGFCLASPSLVLFHNFTLKLAASVGAIVVSVAYRLAPEHRLPAAYEDCVTALQWVSSHAVDGGNFEHDAWLDSHADFSAVYLL GDSAGGNLAHHVVARCAVVEAGSPMRVSGAILLQPFFGGEERTRSEGECPREAFLNLELNDAYWRLALPMGSDRDHPFSNPWNPAAPNLEGVSLPPWLVV IGGRDMLRDRDHDYCGLLKESGKSVEVVVMEEEEHAFYALQPHSLTSERLMQQISHFISS |
Full Sequence |
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Protein Sequence Length: 355 Download |
MDLAEVENLR GFLKVYSDGT IFRLEDPQMF VKASLQGGET GVVGSTLLAL LLPPTTNRKA 60 PPPANRLFPW RRFLPRVPLA GAFSQLLQQQ TEKRRLPLIV YFHGGGFCLA SPSLVLFHNF 120 TLKLAASVGA IVVSVAYRLA PEHRLPAAYE DCVTALQWVS SHAVDGGNFE HDAWLDSHAD 180 FSAVYLLGDS AGGNLAHHVV ARCAVVEAGS PMRVSGAILL QPFFGGEERT RSEGECPREA 240 FLNLELNDAY WRLALPMGSD RDHPFSNPWN PAAPNLEGVS LPPWLVVIGG RDMLRDRDHD 300 YCGLLKESGK SVEVVVMEEE EHAFYALQPH SLTSERLMQQ ISHFISSSAK SPKSN 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 4.0e-5 | 91 | 282 | 220 | + 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 | 1.0e-6 | 91 | 197 | 118 | + Carboxylesterase family. | ||
PRK10162 | PRK10162 | 1.0e-6 | 99 | 196 | 99 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 1.0e-26 | 58 | 350 | 294 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-54 | 99 | 325 | 227 | + 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 | 348 | 1 | 326 | unknown [Picea sitchensis] |
GenBank | ABK25952.1 | 0 | 1 | 348 | 1 | 326 | unknown [Picea sitchensis] |
GenBank | ABK26127.1 | 0 | 2 | 348 | 14 | 338 | unknown [Picea sitchensis] |
GenBank | ABK26852.1 | 0 | 3 | 346 | 1 | 322 | unknown [Picea sitchensis] |
GenBank | ABK26900.1 | 0 | 1 | 348 | 1 | 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 | 0 | 87 | 347 | 104 | 350 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 2zsh_A | 0 | 87 | 347 | 104 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 0 | 96 | 348 | 112 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 0 | 96 | 348 | 112 | 350 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 0 | 96 | 348 | 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 |
DT625935 | 342 | 8 | 348 | 0 |
DV985337 | 335 | 7 | 340 | 0 |
CO414500 | 335 | 1 | 334 | 0 |
ES661662 | 312 | 1 | 311 | 0 |
CN784365 | 312 | 1 | 311 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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