y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.002G197000.1 |
Family | CE10 |
Protein Properties | Length: 415 Molecular Weight: 45939.8 Isoelectric Point: 8.1966 |
Chromosome | Chromosome/Scaffold: 02 Start: 35461079 End: 35480083 |
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 | 116 | 361 | 1.4013e-45 |
RRSLVYGDQPRNRFDLYLPADIGEPKPVLIFVTGGAWIIGYKAWGSLLGLQLAERGIIVACLDYRNFPQGTISDMVNDTSQGISFIINNIANYGGDPNRV YLMGQSAGAHISSCALLEQAARESEKGENVSWSISQIKAYFGLSGGYNLLDLVDHFHKRGLYRRIFLSIMEGEESLKVFSPEIKIQEPCLKSVIPHFPPV YLVHGTADYSIPSVASERFADALQKAGARAELILCEGKTHTDLFLQ |
Full Sequence |
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Protein Sequence Length: 415 Download |
MAALTNRRRT LPPDDVGSQA ITADSVSANY LTTHHLANGK TGLRPPLARQ ESLRRNIEHV 60 AAETYLITRL AFTLLRYLGI GYLWISQLLA LGCYAVLLMP GFLQVAYEYF SSTKVRRSLV 120 YGDQPRNRFD LYLPADIGEP KPVLIFVTGG AWIIGYKAWG SLLGLQLAER GIIVACLDYR 180 NFPQGTISDM VNDTSQGISF IINNIANYGG DPNRVYLMGQ SAGAHISSCA LLEQAARESE 240 KGENVSWSIS QIKAYFGLSG GYNLLDLVDH FHKRGLYRRI FLSIMEGEES LKVFSPEIKI 300 QEPCLKSVIP HFPPVYLVHG TADYSIPSVA SERFADALQK AGARAELILC EGKTHTDLFL 360 QDPLRGGNDY LFDHAVAIIH SNDSDALTKD VFAPRRKRFV PEILLKLASK ISPF* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 5.0e-8 | 130 | 237 | 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. | ||
pfam00135 | COesterase | 3.0e-9 | 131 | 237 | 130 | + Carboxylesterase family. | ||
COG2272 | PnbA | 9.0e-12 | 130 | 232 | 118 | + Carboxylesterase type B [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 9.0e-12 | 144 | 355 | 218 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG0657 | Aes | 6.0e-23 | 116 | 355 | 246 | + 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 | 44 | 414 | 58 | 427 | hypothetical protein [Cleome spinosa] |
RefSeq | NP_186890.2 | 0 | 45 | 414 | 54 | 422 | unknown protein [Arabidopsis thaliana] |
RefSeq | NP_197090.2 | 0 | 49 | 414 | 63 | 427 | ATPCME (PRENYLCYSTEINE METHYLESTERASE); prenylcysteine methylesterase [Arabidopsis thaliana] |
RefSeq | XP_002264962.1 | 0 | 46 | 414 | 50 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329262.1 | 0 | 50 | 414 | 13 | 377 | predicted protein [Populus trichocarpa] |
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 | 0.00000001 | 131 | 355 | 64 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.00000002 | 131 | 355 | 64 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 2pbl_D | 0.00000003 | 114 | 226 | 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 | 0.00000003 | 114 | 226 | 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 | 0.00000003 | 114 | 226 | 38 | 142 | A Chain A, Crystal Structure Of A Putative Thioesterase (Tm1040_2492) From Silicibacter Sp. Tm1040 At 1.79 A Resolution |