| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s74_172V6.1 |
| Family | CE10 |
| Protein Properties | Length: 412 Molecular Weight: 45738.4 Isoelectric Point: 7.9997 |
| Chromosome | Chromosome/Scaffold: 74 Start: 1079094 End: 1082383 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 185 | 398 | 1.2e-35 |
| LVYGDHPRNRFDLFLPTGGHKPRPAVIFVTGGAWVIGYKAWGALLARQLAERNIIVACIDYRNFPQGSVSDMVSDVSRGIGHLCQNIGDPNIGGDPNKIY LVGQSAGAHLGACALLLQAEKQITDGTAGLTWISSQIKAYVALSGGYNLRNLMEHFDRRGLYKSLFLRIMKDEEGLTRFSPECIVRSPSFRDAVALLPPI TLVHGTADYSIPYE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 412 Download |
| MPSSVTANSE SSPVVAPQEM DVSYGSRSVR RASDPGYTRV AVHDREEIEE VDTVINVDDL 60 LRSRQFTSDG APERSLAGEE YGNRTCSERQ DSVRSLTEEV QHIASETSLI TRLSLTLLRF 120 LGTKHTASVC FVSVSNYPVL ILFDRVGTRW IAKFIRLGVY ALCLMPGFIQ VMYYYFFSKN 180 IQRSLVYGDH PRNRFDLFLP TGGHKPRPAV IFVTGGAWVI GYKAWGALLA RQLAERNIIV 240 ACIDYRNFPQ GSVSDMVSDV SRGIGHLCQN IGDPNIGGDP NKIYLVGQSA GAHLGACALL 300 LQAEKQITDG TAGLTWISSQ IKAYVALSGG YNLRNLMEHF DRRGLYKSLF LRIMKDEEGL 360 TRFSPECIVR SPSFRDAVAL LPPITLVHGT ADYSIPYEAR CLIRSLIYFI M* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07859 | Abhydrolase_3 | 0.005 | 210 | 392 | 197 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG2272 | PnbA | 0.003 | 196 | 289 | 111 | + Carboxylesterase type B [Lipid metabolism] | ||
| cd00312 | Esterase_lipase | 0.001 | 205 | 289 | 95 | + 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. | ||
| COG1506 | DAP2 | 0.001 | 205 | 398 | 211 | + Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism] | ||
| COG0657 | Aes | 9.0e-12 | 185 | 396 | 219 | + 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 |
| RefSeq | XP_001763711.1 | 0 | 73 | 399 | 4 | 317 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001765210.1 | 0 | 73 | 399 | 4 | 308 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001775734.1 | 0 | 74 | 397 | 16 | 315 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002329262.1 | 0 | 84 | 399 | 4 | 293 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514516.1 | 0 | 54 | 399 | 45 | 361 | catalytic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2pbl_D | 0.0000002 | 184 | 299 | 42 | 147 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2pbl_C | 0.0000002 | 184 | 299 | 42 | 147 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2pbl_B | 0.0000002 | 184 | 299 | 42 | 147 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2pbl_A | 0.0000002 | 184 | 299 | 42 | 147 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2hm7_A | 0.000001 | 197 | 305 | 64 | 171 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
