Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G406177_T01 |
Family | CE10 |
Protein Properties | Length: 391 Molecular Weight: 42719.6 Isoelectric Point: 7.0699 |
Chromosome | Chromosome/Scaffold: 8 Start: 73688838 End: 73694610 |
Description | prenylcysteine methylesterase |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 161 | 355 | 4e-32 |
PQGTISDMVSDASEAISFICNNVVSFGGDPNKIYLMGQSAGAHIAACALLEQAIKESKGENTYWNVAQIKAYFGLSGGYNIQNLVDHFHERGLYRSIFLS IMEGEESLPHYSPEIVAKKLSAETISLLPQIVLLHGTADYSIPSSASETFADVLKQAGGKVELQLYKGKTHTDVFLQDPLRGGRDKLVEDVLSVI |
Full Sequence |
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Protein Sequence Length: 391 Download |
MQLASEHPAC GRASAEGEAF VPRSGAQGLR RRTGAAPLDY SSPRSGRAGD GKRTTFREDV 60 GHAAAETYLV TGLAFTLLGY LGVSYRWISQ LIALLVYAVL LMPGFIKVGY YYFFSRHVIR 120 SVIYGEQPRN RLDLYIPKDN SKSSPVVAFV TGGAWIIGNF PQGTISDMVS DASEAISFIC 180 NNVVSFGGDP NKIYLMGQSA GAHIAACALL EQAIKESKGE NTYWNVAQIK AYFGLSGGYN 240 IQNLVDHFHE RGLYRSIFLS IMEGEESLPH YSPEIVAKKL SAETISLLPQ IVLLHGTADY 300 SIPSSASETF ADVLKQAGGK VELQLYKGKT HTDVFLQDPL RGGRDKLVED VLSVIHVDDA 360 SARERDASAP TPERLVYEWQ IKLARQISPF * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG2272 | PnbA | 3.0e-6 | 132 | 219 | 127 | + Carboxylesterase type B [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-6 | 171 | 331 | 170 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
cd00312 | Esterase_lipase | 2.0e-7 | 132 | 228 | 141 | + 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 | 4.0e-8 | 132 | 210 | 119 | + Carboxylesterase family. | ||
COG0657 | Aes | 2.0e-17 | 124 | 347 | 262 | + 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 | 15 | 390 | 25 | 427 | hypothetical protein [Cleome spinosa] |
GenBank | EAY99150.1 | 0 | 8 | 390 | 75 | 458 | hypothetical protein OsI_21109 [Oryza sativa Indica Group] |
GenBank | EEE55068.1 | 0 | 37 | 390 | 28 | 409 | hypothetical protein OsJ_02788 [Oryza sativa Japonica Group] |
RefSeq | NP_001056406.1 | 0 | 1 | 390 | 1 | 414 | Os05g0577200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001132117.1 | 0 | 12 | 390 | 2 | 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 | 0.0002 | 131 | 331 | 61 | 282 | A Chain A, Crystal Structure Analysis Of The G84s Est2 Mutant |
PDB | 1evq_A | 0.0002 | 131 | 331 | 61 | 282 | A Chain A, The Crystal Structure Of The Thermophilic Carboxylesterase Est2 From Alicyclobacillus Acidocaldarius |
PDB | 1jmy_A | 0.0006 | 125 | 201 | 127 | 196 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
PDB | 4e15_B | 0.0008 | 124 | 334 | 63 | 282 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
PDB | 4e15_A | 0.0008 | 124 | 334 | 63 | 282 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |