y
Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT1G26120.1 |
Family | CE10 |
Protein Properties | Length: 477 Molecular Weight: 52718.7 Isoelectric Point: 6.8379 |
Chromosome | Chromosome/Scaffold: 1 Start: 9028395 End: 9031485 |
Description | serine esterase, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 181 | 428 | 0 |
RRSIVYGDQPRNRLDLYLPKNSTGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGSISDMVKDASSGISFVCNHIAEYGGDPDRI YLMGQSAGAHIAACTIVEQVIKESGEGDSVSWSSSQINAYFGLSGGYNLLNLVDHFHSRGLYRSIFLSIMEGEESLRQFSPELVVQNPNLKHIIARLPPF ILFHGTDDYSIPSDASKSFAETLQRLGAKAKVILYEGKTHTDLFLQDP |
Full Sequence |
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Protein Sequence Length: 477 Download |
MPSQILQISH HLPPKSSPST EMMFKSLIYD DPSTTLLSRF GDDHHTISST VKPLLSRSSS 60 YNGTAMKTSS SSSAGGFTGW YQNRRRRSNS DNCLSAFSDD TNGTADGGNN SGDRQTTIGQ 120 EVGHAAAETF LLTRLCLKLL SYLGVGYRWI TRFMALGCYA FLLMPGFIQV GYYYFFSPYV 180 RRSIVYGDQP RNRLDLYLPK NSTGPKPVVA FVTGGAWIIG YKAWGSLLGQ QLSERDIIVA 240 CIDYRNFPQG SISDMVKDAS SGISFVCNHI AEYGGDPDRI YLMGQSAGAH IAACTIVEQV 300 IKESGEGDSV SWSSSQINAY FGLSGGYNLL NLVDHFHSRG LYRSIFLSIM EGEESLRQFS 360 PELVVQNPNL KHIIARLPPF ILFHGTDDYS IPSDASKSFA ETLQRLGAKA KVILYEGKTH 420 TDLFLQDPMR GGIDEMFEDI VTVVLGDDQE AIGKSVDRRR LVPEFMLKLA HWVSPF* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 6.0e-8 | 194 | 289 | 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 | 3.0e-9 | 196 | 293 | 119 | + Carboxylesterase family. | ||
pfam07859 | Abhydrolase_3 | 5.0e-10 | 214 | 420 | 213 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG2272 | PnbA | 3.0e-10 | 194 | 293 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 4.0e-23 | 181 | 420 | 247 | + Esterase/lipase [Lipid metabolism] |
Gene Ontology | |
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GO Term | Description |
GO:0005575 | cellular_component |
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 | 476 | 1 | 472 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
DDBJ | BAH56976.1 | 0 | 1 | 326 | 1 | 326 | AT1G26120 [Arabidopsis thaliana] |
RefSeq | NP_173937.2 | 0 | 1 | 476 | 1 | 476 | esterase-related [Arabidopsis thaliana] |
RefSeq | XP_002277990.1 | 0 | 17 | 476 | 12 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514516.1 | 0 | 13 | 476 | 30 | 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 | 2c7b_B | 0.00000000008 | 193 | 420 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.00000000008 | 193 | 420 | 61 | 281 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2hm7_A | 0.0000000005 | 193 | 420 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.0000000007 | 193 | 420 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1lzl_A | 0.0000000009 | 189 | 298 | 62 | 172 | A Chain A, Bacterial Heroin Esterase |