y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00033569m |
Family | CE10 |
Protein Properties | Length: 417 Molecular Weight: 45297.7 Isoelectric Point: 7.371 |
Chromosome | Chromosome/Scaffold: 027142 Start: 1529 End: 6419 |
Description | prenylcysteine methylesterase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 120 | 382 | 0 |
VVYGEQPRNRKVMLDLYIPKDHSKSCPVVAFVTGGAWIIGYKAWGALLGRRLAERGIIVACIDYRNFPQGTISDMVTDASEGISFVCNNAVSFGGDPNKI YLMGQSAGAHIAACALLDQAVKESKGEHTSWNMAQVKAYFGLSGGYNIQNLVNHFHERGLYRSIFLSIMEGEESLPHFSPEIVTKKSSAEAIALLPEIVL MHGTADYSIPSSASETFADVLKQAGGKVKLKLYEGKTHTDVFLQDPLRGGRDQLVEDVISVIH |
Full Sequence |
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Protein Sequence Length: 417 Download |
MQPGGQTSGG DAGAEAEAFV PVGGLHGLRR RTGPVSLDSS PRSGRAGDGR RSTFREDVGH 60 AAAETYLVTG LAFTLLGYLG VGYRWISQLI ALLLYAVLLM PGFIKVGYYY FFSSQVCRSV 120 VYGEQPRNRK VMLDLYIPKD HSKSCPVVAF VTGGAWIIGY KAWGALLGRR LAERGIIVAC 180 IDYRNFPQGT ISDMVTDASE GISFVCNNAV SFGGDPNKIY LMGQSAGAHI AACALLDQAV 240 KESKGEHTSW NMAQVKAYFG LSGGYNIQNL VNHFHERGLY RSIFLSIMEG EESLPHFSPE 300 IVTKKSSAEA IALLPEIVLM HGTADYSIPS SASETFADVL KQAGGKVKLK LYEGKTHTDV 360 FLQDPLRGGR DQLVEDVISV IHADDAHARE KDALAPTPER LVYEWQIKLA RQISPF* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07859 | Abhydrolase_3 | 1.0e-9 | 153 | 357 | 215 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
cd00312 | Esterase_lipase | 3.0e-10 | 133 | 241 | 122 | + 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. | ||
COG2272 | PnbA | 2.0e-11 | 133 | 245 | 127 | + Carboxylesterase type B [Lipid metabolism] | ||
pfam00135 | COesterase | 8.0e-12 | 133 | 236 | 123 | + Carboxylesterase family. | ||
COG0657 | Aes | 4.0e-21 | 126 | 357 | 245 | + 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 | ABD96862.1 | 0 | 14 | 416 | 25 | 427 | hypothetical protein [Cleome spinosa] |
GenBank | EAY99150.1 | 0 | 2 | 416 | 71 | 458 | hypothetical protein OsI_21109 [Oryza sativa Indica Group] |
GenBank | EEE55068.1 | 0 | 39 | 416 | 32 | 409 | hypothetical protein OsJ_02788 [Oryza sativa Japonica Group] |
RefSeq | NP_001056406.1 | 0 | 1 | 416 | 1 | 414 | Os05g0577200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001132117.1 | 0 | 15 | 416 | 7 | 404 | hypothetical protein LOC100193534 [Zea mays] |
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 | 2hm7_A | 0.0000000001 | 129 | 357 | 58 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.0000000001 | 129 | 357 | 58 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1u4n_A | 0.000000001 | 129 | 357 | 58 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1qz3_A | 0.000000001 | 129 | 357 | 58 | 282 | A Chain A, Crystal Structure Of Mutant M211sR215L OF CARBOXYLESTERASE Est2 Complexed With Hexadecanesulfonate |
PDB | 1qe3_A | 0.000000006 | 119 | 248 | 69 | 220 | A Chain A, Pnb Esterase |