y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.013G079100.2 |
Family | CE10 |
Protein Properties | Length: 415 Molecular Weight: 45618.1 Isoelectric Point: 8.1904 |
Chromosome | Chromosome/Scaffold: 13 Start: 10561752 End: 10567191 |
Description | prenylcysteine methylesterase |
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 | 162 | 313 | 5.3e-37 |
QVRRSIIYGEKPRNRLDLYLPKTSQGTKPVVAFITGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGTISDMVEDASQGISFICNNISEYGGDPN RIYLMGQSAGAHIAACTLVNQAIKETGEGDSVSWSVSQIKAYLGLSGGYNLF |
Full Sequence |
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Protein Sequence Length: 415 Download |
MPSPILPISS HPSSSASAAT TVVKAKIDAD PSATILISSK FDPEKAIPIT PVLPRASSYN 60 STSNVNNNIV SFANNHQQRF LRTSSDSSLA LLADETPRQS ISREVGHVAA ETFYLSGLCL 120 KLLSYLGVGY RWITRFLALG CYAMLLMPGF IQVAFYYFFS RQVRRSIIYG EKPRNRLDLY 180 LPKTSQGTKP VVAFITGGAW IIGYKAWGSL LGQQLSERDI IVACIDYRNF PQGTISDMVE 240 DASQGISFIC NNISEYGGDP NRIYLMGQSA GAHIAACTLV NQAIKETGEG DSVSWSVSQI 300 KAYLGLSGGY NLFNLIEHFH TRGLYRSIFL SQNFADTLRR VGGKAESILY YGKTHTDLFL 360 QDPMRGGRDE MFEDVVAIIH GEDEAALAKD AVAPPRRRLV PEFMLKLAHD VSPF* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07859 | Abhydrolase_3 | 4.0e-8 | 194 | 280 | 88 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
cd00312 | Esterase_lipase | 2.0e-8 | 177 | 272 | 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 | 9.0e-10 | 179 | 284 | 142 | + Carboxylesterase family. | ||
COG2272 | PnbA | 8.0e-10 | 177 | 276 | 114 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 1.0e-17 | 164 | 276 | 115 | + 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 | 414 | 1 | 472 | AC084221_10 hypothetical protein [Arabidopsis thaliana] |
RefSeq | NP_173937.2 | 0 | 1 | 414 | 1 | 476 | esterase-related [Arabidopsis thaliana] |
RefSeq | XP_002264962.1 | 0 | 98 | 414 | 53 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277990.1 | 0 | 1 | 414 | 1 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514516.1 | 0 | 2 | 414 | 4 | 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 | 0.000000003 | 176 | 278 | 61 | 163 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.000000003 | 176 | 278 | 61 | 163 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 1c7i_A | 0.00000007 | 166 | 288 | 69 | 216 | A Chain A, Thermophylic Pnb Esterase |
PDB | 1c7j_A | 0.00000008 | 166 | 288 | 69 | 216 | A Chain A, Pnb Esterase 56c8 |
PDB | 1qe3_A | 0.00000008 | 166 | 288 | 69 | 216 | A Chain A, Pnb Esterase |