| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s62_226V6.1 |
| Family | CE10 |
| Protein Properties | Length: 517 Molecular Weight: 57042.6 Isoelectric Point: 8.5087 |
| Chromosome | Chromosome/Scaffold: 62 Start: 1710881 End: 1716229 |
| Description | prenylcysteine methylesterase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 218 | 464 | 8.70206e-43 |
| SLIYGEKPRNRFDLYLPPDTDKLKPVFIFITGGAWVIGYKAWGTLLAQQLVDCDIIVACIDYRNFPQGGISDMISDVETGIGYVIQKLESYGGDPNMVYL AGQSAGAHLATCALLKQAEKEITQDPADLVWRSSQIKECMAISGGYNLTKLVDHFHKRGLYKSIFLSMVEGEKSLATYSPELMVLAPSFRKAVPLLPPIT LYHGTADYSIPHDSSVAFAVALRLVGARVNTVFYPNKTHTDLFLQDP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 517 Download |
| MAKRDLEEVV EMLPAEEIQN DTMMLRSGWG LEAPSAGLLR HGGSRMTSAK VQGDGFVCVG 60 SVKLRSTASG AMKTDVGLQQ EAVGVGAEDR DREDGNHRKV LRFQSEVAAR GVPRLSSQRT 120 PLAGAEHGRR RTFSGPSQFG GGGPLRQGSF KEFTQDVQAA AAETYLITRL ALTLLKFLGV 180 GTRWISKFIR LSLYAMFLMI GFIQVGYSYY YDPRIHRSLI YGEKPRNRFD LYLPPDTDKL 240 KPVFIFITGG AWVIGYKAWG TLLAQQLVDC DIIVACIDYR NFPQGGISDM ISDVETGIGY 300 VIQKLESYGG DPNMVYLAGQ SAGAHLATCA LLKQAEKEIT QDPADLVWRS SQIKECMAIS 360 GGYNLTKLVD HFHKRGLYKS IFLSMVEGEK SLATYSPELM VLAPSFRKAV PLLPPITLYH 420 GTADYSIPHD SSVAFAVALR LVGARVNTVF YPNKTHTDLF LQDPMRGGKD ELLADILAVV 480 HANDEEAKAE DVKRAYCRRR LVPEFLLQLA RLVSPF* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 2.0e-5 | 230 | 337 | 121 | + 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 | 3.0e-8 | 231 | 456 | 245 | + Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism] | ||
| COG2272 | PnbA | 1.0e-8 | 230 | 333 | 121 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 6.0e-12 | 244 | 456 | 223 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| COG0657 | Aes | 1.0e-18 | 221 | 456 | 249 | + 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 | NP_197090.2 | 0 | 112 | 516 | 28 | 427 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
| RefSeq | XP_001763711.1 | 0 | 118 | 516 | 3 | 402 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001765210.1 | 0 | 118 | 516 | 3 | 391 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001775734.1 | 0 | 115 | 516 | 1 | 402 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002514516.1 | 0 | 151 | 516 | 82 | 445 | 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 | 1lzl_A | 0.000003 | 225 | 456 | 63 | 290 | A Chain A, Bacterial Heroin Esterase |
| PDB | 1lzk_A | 0.000003 | 225 | 456 | 63 | 290 | A Chain A, Bacterial Heroin Esterase Complex With Transition State Analog Dimethylarsenic Acid |
| PDB | 2pbl_D | 0.000008 | 214 | 326 | 38 | 142 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2pbl_C | 0.000008 | 214 | 326 | 38 | 142 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
| PDB | 2pbl_B | 0.000008 | 214 | 326 | 38 | 142 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |
