Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G473976_T01 |
Family | CE10 |
Protein Properties | Length: 405 Molecular Weight: 44500.8 Isoelectric Point: 8.2027 |
Chromosome | Chromosome/Scaffold: 3 Start: 215081404 End: 215089219 |
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 | 106 | 364 | 0 |
QVRRSVVYGDQPRNRLDLYIPEDNSRPCPVVAFVTGGAWIIGYKAWGALLGRRLAERGIIVACIDYRNFPQGTIGDMVHDASQGISFVCNNIASHGGDPN QIYLIGQSAGAHIAACALMEQAVKESGGNPVSWSLTQIKAYFGLSGGYNMHNLVDHFHERGLNRSIFLSIMEGEESLSRYSPEIVAKTSSAETIALLPLV VLMHGTEDYSIPSSSSQTFVDVLQQAGAQARLLLYEGKTHTDIFVQDPLRGGRDPLVED |
Full Sequence |
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Protein Sequence Length: 405 Download |
MRASVEEAGA LLARSDSAGR RRRSPPPVQT ASPRPGSLRR QSSSFREDVG HAASETYLVS 60 RLTFTLLQYL GLGYRWMSQL LSLTIYAIVL MPGFIQVGYY YFFSSQVRRS VVYGDQPRNR 120 LDLYIPEDNS RPCPVVAFVT GGAWIIGYKA WGALLGRRLA ERGIIVACID YRNFPQGTIG 180 DMVHDASQGI SFVCNNIASH GGDPNQIYLI GQSAGAHIAA CALMEQAVKE SGGNPVSWSL 240 TQIKAYFGLS GGYNMHNLVD HFHERGLNRS IFLSIMEGEE SLSRYSPEIV AKTSSAETIA 300 LLPLVVLMHG TEDYSIPSSS SQTFVDVLQQ AGAQARLLLY EGKTHTDIFV QDPLRGGRDP 360 LVEDVLSIIH ADDANACQKI ALAPTPRRLV FEWQLKLARK ISPF* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07859 | Abhydrolase_3 | 4.0e-7 | 141 | 236 | 97 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
cd00312 | Esterase_lipase | 2.0e-8 | 121 | 229 | 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 | 6.0e-11 | 121 | 242 | 142 | + Carboxylesterase family. | ||
COG2272 | PnbA | 4.0e-13 | 121 | 224 | 118 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 9.0e-19 | 108 | 224 | 119 | + 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 | EEC71166.1 | 0 | 72 | 404 | 4 | 342 | hypothetical protein OsI_03031 [Oryza sativa Indica Group] |
GenBank | EEE55068.1 | 0 | 3 | 404 | 5 | 409 | hypothetical protein OsJ_02788 [Oryza sativa Japonica Group] |
RefSeq | NP_001056406.1 | 0 | 21 | 404 | 29 | 414 | Os05g0577200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001132117.1 | 0 | 1 | 404 | 1 | 404 | hypothetical protein LOC100193534 [Zea mays] |
RefSeq | XP_002456038.1 | 0 | 1 | 335 | 1 | 339 | hypothetical protein SORBIDRAFT_03g029280 [Sorghum bicolor] |
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 | 1jmy_A | 0.0000000009 | 105 | 239 | 67 | 237 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
PDB | 1f6w_A | 0.000000002 | 105 | 239 | 67 | 237 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 4e15_B | 0.000000003 | 113 | 348 | 63 | 282 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 4e15_A | 0.000000003 | 113 | 348 | 63 | 282 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 4e14_A | 0.000000003 | 113 | 348 | 63 | 282 | A Chain A, Crystal Structure Of Kynurenine Formamidase Conjugated With Phenylmethylsulfonyl Fluoride |