| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s131_174V6.1 |
| Family | CE10 |
| Protein Properties | Length: 421 Molecular Weight: 46613.6 Isoelectric Point: 7.1092 |
| Chromosome | Chromosome/Scaffold: 131 Start: 1039658 End: 1042934 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 117 | 385 | 1.9e-33 |
| IARNVRFSQAQRNLLDVYVPNRKSAVGVGLKPVVLFVHGGVWASGDKWQFSPLGTFLAESGVIAVLVQYTLYPEVLAIDQVSEVSCALTWTMDNIAQYGG DPERVFLMGHSSGAHLSSMMLWERASRLVKNAERPIPEQLDLRIPYGYLGLAGVYNISEHFKYEASRGVEAISCMRPAMGWEESFDSMSPTLLFGALLMQ GGASFATNRYTDTTTEIQVRGLNLAPKCLFLASREDLVVPPTSSLAINSVLQTLGCDSRVIVYEDLKHE | |||
| Full Sequence |
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| Protein Sequence Length: 421 Download |
| MAMKADMVDE AFAPPSARRS APGRMPVNAG MLGEAVKGAV REAFQIRDVG PLHRVLILFG 60 LLFTIAREVL GTIKLAPYGA YAYRTYVSLP PWRKHETQDS LPPTRRWWSH NTHDVAIARN 120 VRFSQAQRNL LDVYVPNRKS AVGVGLKPVV LFVHGGVWAS GDKWQFSPLG TFLAESGVIA 180 VLVQYTLYPE VLAIDQVSEV SCALTWTMDN IAQYGGDPER VFLMGHSSGA HLSSMMLWER 240 ASRLVKNAER PIPEQLDLRI PYGYLGLAGV YNISEHFKYE ASRGVEAISC MRPAMGWEES 300 FDSMSPTLLF GALLMQGGAS FATNRYTDTT TEIQVRGLNL APKCLFLASR EDLVVPPTSS 360 LAINSVLQTL GCDSRVIVYE DLKHEDFVLW HKGWGTLKSH VGSYLEEILK FVMVESSSND 420 * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG2272 | PnbA | 4.0e-11 | 131 | 237 | 121 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-11 | 150 | 246 | 102 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| cd00312 | Esterase_lipase | 8.0e-12 | 131 | 248 | 132 | + 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 | 2.0e-14 | 131 | 248 | 134 | + Carboxylesterase family. | ||
| COG0657 | Aes | 6.0e-19 | 131 | 248 | 120 | + Esterase/lipase [Lipid metabolism] | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAL52944.1 | 0 | 61 | 406 | 297 | 645 | inositol phosphatase-like protein (ISS) [Ostreococcus tauri] |
| GenBank | EEH53145.1 | 2e-38 | 68 | 342 | 37 | 361 | predicted protein [Micromonas pusilla CCMP1545] |
| RefSeq | XP_001416958.1 | 0 | 68 | 414 | 3 | 356 | predicted protein [Ostreococcus lucimarinus CCE9901] |
| RefSeq | XP_001770966.1 | 0 | 1 | 420 | 67 | 486 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002501244.1 | 0 | 68 | 306 | 14 | 267 | predicted protein [Micromonas sp. RCC299] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bl8_D | 0.00000005 | 84 | 243 | 58 | 242 | A Chain A, Crystal Structure Of The Extracellular Domain Of Neuroligin 2a From Mouse |
| PDB | 3bl8_C | 0.00000005 | 84 | 243 | 58 | 242 | A Chain A, Crystal Structure Of The Extracellular Domain Of Neuroligin 2a From Mouse |
| PDB | 3bl8_B | 0.00000005 | 84 | 243 | 58 | 242 | A Chain A, Crystal Structure Of The Extracellular Domain Of Neuroligin 2a From Mouse |
| PDB | 3bl8_A | 0.00000005 | 84 | 243 | 58 | 242 | A Chain A, Crystal Structure Of The Extracellular Domain Of Neuroligin 2a From Mouse |
| PDB | 2pbl_D | 0.0000007 | 120 | 237 | 42 | 147 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| FC361972 | 265 | 26 | 290 | 0 |
| BY992514 | 261 | 1 | 261 | 0 |
| DC934496 | 232 | 65 | 296 | 0 |
| DC948628 | 221 | 201 | 421 | 0 |
| FC361971 | 208 | 214 | 421 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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