y
Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a006071m |
Family | CE10 |
Protein Properties | Length: 459 Molecular Weight: 50552.7 Isoelectric Point: 9.2061 |
Chromosome | Chromosome/Scaffold: 37 Start: 1702948 End: 1706355 |
Description | alpha/beta-Hydrolases superfamily protein |
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 | 163 | 417 | 0 |
GVIYGDQPRNRLDLYLPKNRNGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGTIGDMVKDASQGISFVCNIIAEYGGDPNNVYL MGQSAGAHIASCALLEQAIKEARGEKTSWSVSRIKAYFGLSGGYNLFNLVDHFHSRGLYRSIFLSIMEGEESLRRYSPEVMVRDPNNKGAVSLLPRTVLF HGTADYSIPSDSSKNFAEVLQSMGVEAESVLYEGKTHTDLFLQDPMRGGRDDLFE |
Full Sequence |
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Protein Sequence Length: 459 Download |
MIETASAAAA ASARMLLGSE DELRGDATKI TIPPSSAADD DDKEIESKPL ISRSLSYTYA 60 PPSAALTAKP NLNQKQRRRR VASDTSSIFT PSAARRQPFR QMGRAASDTY LITRLSFKLL 120 GYLGVGYRWI LRFLALGCYA VLLFPGFIQV GYYYFFSSQI RRGVIYGDQP RNRLDLYLPK 180 NRNGPKPVVA FVTGGAWIIG YKAWGSLLGQ QLSERDIIVA CIDYRNFPQG TIGDMVKDAS 240 QGISFVCNII AEYGGDPNNV YLMGQSAGAH IASCALLEQA IKEARGEKTS WSVSRIKAYF 300 GLSGGYNLFN LVDHFHSRGL YRSIFLSIME GEESLRRYSP EVMVRDPNNK GAVSLLPRTV 360 LFHGTADYSI PSDSSKNFAE VLQSMGVEAE SVLYEGKTHT DLFLQDPMRG GRDDLFEDLV 420 GMIHAGDSEA AAKDAKATPR KRLVPELMLR LARIVSPF* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 2.0e-8 | 174 | 282 | 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 | 4.0e-10 | 176 | 277 | 123 | + Carboxylesterase family. | ||
COG2272 | PnbA | 1.0e-10 | 174 | 286 | 127 | + Carboxylesterase type B [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 7.0e-11 | 194 | 399 | 212 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG0657 | Aes | 2.0e-21 | 166 | 399 | 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 | 75 | 458 | 43 | 427 | hypothetical protein [Cleome spinosa] |
RefSeq | XP_002264962.1 | 0 | 30 | 458 | 1 | 417 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277990.1 | 0 | 1 | 458 | 17 | 458 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315969.1 | 0 | 36 | 458 | 44 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514516.1 | 0 | 3 | 458 | 27 | 445 | catalytic, putative [Ricinus communis] |
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 | 0.000000007 | 156 | 295 | 65 | 231 | A Chain A, Truncated Recombinant Human Bile Salt Stimulated Lipase |
PDB | 1f6w_A | 0.00000003 | 156 | 295 | 65 | 231 | A Chain A, Structure Of The Catalytic Domain Of Human Bile Salt Activated Lipase |
PDB | 2c7b_B | 0.0000005 | 173 | 415 | 61 | 297 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.0000005 | 173 | 415 | 61 | 297 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 1lzl_A | 0.000001 | 169 | 278 | 62 | 172 | A Chain A, Bacterial Heroin Esterase |