| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi2g44942.1 |
| Family | CE10 |
| Protein Properties | Length: 410 Molecular Weight: 45184.5 Isoelectric Point: 8.5234 |
| Chromosome | Chromosome/Scaffold: 2 Start: 45326419 End: 45332549 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 112 | 374 | 0 |
| QVRRSIVYGEQPRNRLDLYIPKDNTRPCPVMAFVTGGAWIIGYKAWGALLGRRLAERGIIVACIDYRNFPQGTISDMVADASQGISFVCNNIASYGGDPN QIYLMGQSAGAHIAACALMEQAVKESSGQPISWSVTQIKAYFGLSGGYNIYNLVDHFHQRGLYRSIFLSIMDGEESLSRYSPEIVVKESSPQTIALLPPI VLMHGTDDYSIPSSASQTFVDVLQQVGAQARLLLYEGKTHTDIFLQDPLRGGKDPLVEDVLSV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 410 Download |
| MQPPSSGGDA READALLARS DSAGRRRRAS PVQSASPAPQ GWGGPRRQSS FRDDVGHAAS 60 ETYLVTRLTF TLLQYLGLGY RWMTQLLALA VYAILLMPGF LQVGYYYFFS SQVRRSIVYG 120 EQPRNRLDLY IPKDNTRPCP VMAFVTGGAW IIGYKAWGAL LGRRLAERGI IVACIDYRNF 180 PQGTISDMVA DASQGISFVC NNIASYGGDP NQIYLMGQSA GAHIAACALM EQAVKESSGQ 240 PISWSVTQIK AYFGLSGGYN IYNLVDHFHQ RGLYRSIFLS IMDGEESLSR YSPEIVVKES 300 SPQTIALLPP IVLMHGTDDY SIPSSASQTF VDVLQQVGAQ ARLLLYEGKT HTDIFLQDPL 360 RGGKDPLVED VLSVIHTDDA TRRNIASAPT PRRLVFEWQL QLARRISPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07859 | Abhydrolase_3 | 3.0e-8 | 147 | 351 | 211 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| cd00312 | Esterase_lipase | 3.0e-10 | 127 | 248 | 142 | + 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-12 | 127 | 226 | 119 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 6.0e-13 | 127 | 230 | 122 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 1.0e-22 | 114 | 351 | 243 | + Esterase/lipase [Lipid metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC71166.1 | 0 | 78 | 409 | 4 | 342 | hypothetical protein OsI_03031 [Oryza sativa Indica Group] |
| GenBank | EEE55068.1 | 0 | 1 | 409 | 1 | 409 | hypothetical protein OsJ_02788 [Oryza sativa Japonica Group] |
| RefSeq | NP_001043688.1 | 0 | 1 | 326 | 1 | 325 | Os01g0642000 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001056406.1 | 0 | 1 | 409 | 1 | 414 | Os05g0577200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001132117.1 | 0 | 12 | 409 | 7 | 404 | hypothetical protein LOC100193534 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1jmy_A | 0.0000000008 | 111 | 222 | 67 | 197 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
| PDB | 1c7i_A | 0.000000002 | 116 | 237 | 69 | 215 | A Chain A, Thermophylic Pnb Esterase |
| PDB | 1qe3_A | 0.000000002 | 116 | 237 | 69 | 215 | A Chain A, Pnb Esterase |
| PDB | 1c7j_A | 0.000000003 | 116 | 237 | 69 | 215 | A Chain A, Pnb Esterase 56c8 |
| PDB | 1f6w_A | 0.000000003 | 111 | 221 | 67 | 196 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
