y
Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre02.g119100.t1.2 |
Family | CE10 |
Protein Properties | Length: 539 Molecular Weight: 55269.1 Isoelectric Point: 6.7695 |
Chromosome | Chromosome/Scaffold: 2 Start: 6820583 End: 6823915 |
Description | alpha/beta-Hydrolases superfamily protein |
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 | 107 | 487 | 1.6e-38 |
VLYGDKPRQRLDLYYPPSSRGAPATTEGATYPLVIYVTGGAWTIGYKAWGALLGRRLSEQGVLVACLDYRNFPQGDALDMLEDVNTGICWVLRRVHRLGG DPDNVTLVGQSAGGHLAGLSLLRQAEQAASGRSALGATPSWSPGCIKAFVGVSGAFDLVGLASHRGGTFRGLLDRILAVDASGMSSADGGGGGAARGVVQ GIVTTAAVSASEVAAAATLSAEDRDAPPPGGPAVPPALPDIEQGGGGGSAAVSSAIIAQGSDKHGETPLLRSPVSSSAPGSLADGQAPAGAAAGGAMAGT RRGGTRVPAYDALSPLEAARRMGSDAAALLPDVLLVHGTADKTVPCEGSARLAEALQAAGATRPVRCVLVPGKTHTAFLLE |
Full Sequence |
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Protein Sequence Length: 539 Download |
MDDDDPGQVV GPRWPPGAPD DLTVPIITSS EPVLGPRTRE HATASQRWCR PFRAVWNALS 60 AVVHVVVLVF KIIHIVLALA VYSMLLLPGF LRMIYYYFFN KCVVRGVLYG DKPRQRLDLY 120 YPPSSRGAPA TTEGATYPLV IYVTGGAWTI GYKAWGALLG RRLSEQGVLV ACLDYRNFPQ 180 GDALDMLEDV NTGICWVLRR VHRLGGDPDN VTLVGQSAGG HLAGLSLLRQ AEQAASGRSA 240 LGATPSWSPG CIKAFVGVSG AFDLVGLASH RGGTFRGLLD RILAVDASGM SSADGGGGGA 300 ARGVVQGIVT TAAVSASEVA AAATLSAEDR DAPPPGGPAV PPALPDIEQG GGGGSAAVSS 360 AIIAQGSDKH GETPLLRSPV SSSAPGSLAD GQAPAGAAAG GAMAGTRRGG TRVPAYDALS 420 PLEAARRMGS DAAALLPDVL LVHGTADKTV PCEGSARLAE ALQAAGATRP VRCVLVPGKT 480 HTAFLLEDPM RGGRDLLMDC VLGAVLGGGE DDPAIGGRVY SSLCPGFLCT AAGWVCPF* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.003 | 117 | 214 | 107 | + 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. | ||
pfam07859 | Abhydrolase_3 | 0.001 | 140 | 214 | 76 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG2272 | PnbA | 0.001 | 138 | 213 | 90 | + Carboxylesterase type B [Lipid metabolism] | ||
COG0657 | Aes | 1.0e-8 | 109 | 214 | 107 | + Esterase/lipase [Lipid metabolism] |
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 | ACG46361.1 | 0 | 70 | 288 | 85 | 293 | carboxylesterase-like protein [Zea mays] |
RefSeq | NP_001146610.1 | 0 | 70 | 282 | 85 | 287 | hypothetical protein LOC100280207 [Zea mays] |
RefSeq | XP_001702446.1 | 0 | 84 | 538 | 1 | 455 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001702447.1 | 0 | 103 | 285 | 53 | 224 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001702447.1 | 0 | 414 | 505 | 230 | 321 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
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 | 2c7b_B | 0.00000004 | 116 | 225 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.00000004 | 116 | 225 | 61 | 162 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 1c7i_A | 0.00000004 | 109 | 220 | 72 | 192 | A Chain A, Thermophylic Pnb Esterase |
PDB | 1c7j_A | 0.00000004 | 109 | 220 | 72 | 192 | A Chain A, Pnb Esterase 56c8 |
PDB | 1qe3_A | 0.00000004 | 109 | 220 | 72 | 192 | A Chain A, Pnb Esterase |