| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre02.g119050.t1.3 |
| Family | CE10 |
| Protein Properties | Length: 551 Molecular Weight: 56843.9 Isoelectric Point: 8.1775 |
| Chromosome | Chromosome/Scaffold: 2 Start: 6816733 End: 6820536 |
| 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 | 119 | 482 | 3.9e-40 |
| VRRSVVYGAKPRQRLDLYYPPSSRTAAHGSVPVVIYITGGAWTIGYKAWGALLGRRLSEQGVLVACLDYRNFPQGDALDMLEDVNTGICWVLRRVHRLGG DPDNVTLVGQSAGGHLAGLSLLRQAEQAASGRSALGATPSWSPGCIKAFVGVSGAFDLVGLAEHLHRRGLYKNLLDRIMSLTTPADVSSTRGGKKVAVAG PHPPPSRTASGCSEGGAGGSYPADAAAVVTTTNSTSSSSCGMGSMIDKGAASGKAGGDSEPSAGSGAGEGSIAVHVGTRHDASGCKGGAEPAYDALSPLA AARRMGSDAAALLPGVLLVHGTADKTVPCEGSARLAEALQTAGATRPVRCLLVPGKTHTAFLLE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 551 Download |
| MVSGVEMGHS GSNGGLTNRQ HQAGDGAGHK PAHDSAASLP PSEPGSMLDL TAPLEHATGL 60 LRRVITEAFL LLRLAVRLWS YLGMGWKWFV QLMRLVLYAA LLLPGFLQMV VFYVFSPRVR 120 RSVVYGAKPR QRLDLYYPPS SRTAAHGSVP VVIYITGGAW TIGYKAWGAL LGRRLSEQGV 180 LVACLDYRNF PQGDALDMLE DVNTGICWVL RRVHRLGGDP DNVTLVGQSA GGHLAGLSLL 240 RQAEQAASGR SALGATPSWS PGCIKAFVGV SGAFDLVGLA EHLHRRGLYK NLLDRIMSLT 300 TPADVSSTRG GKKVAVAGPH PPPSRTASGC SEGGAGGSYP ADAAAVVTTT NSTSSSSCGM 360 GSMIDKGAAS GKAGGDSEPS AGSGAGEGSI AVHVGTRHDA SGCKGGAEPA YDALSPLAAA 420 RRMGSDAAAL LPGVLLVHGT ADKTVPCEGS ARLAEALQTA GATRPVRCLL VPGKTHTAFL 480 LEDPMRGGRD LLMDCVLGAV LGGGEGEGDT GKPVVSVLSA EDAAPPGVRH VYGTLCPGFL 540 CDWAGWVCPF * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10566 | PRK10566 | 0.0009 | 435 | 476 | 42 | + esterase; Provisional | ||
| pfam07859 | Abhydrolase_3 | 0.0008 | 152 | 226 | 76 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| cd00312 | Esterase_lipase | 6.0e-5 | 133 | 226 | 103 | + 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. | ||
| COG2272 | PnbA | 1.0e-5 | 133 | 225 | 107 | + Carboxylesterase type B [Lipid metabolism] | ||
| COG0657 | Aes | 2.0e-9 | 120 | 226 | 108 | + Esterase/lipase [Lipid metabolism] | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_001043688.1 | 0 | 66 | 319 | 59 | 309 | Os01g0642000 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001146610.1 | 0 | 31 | 296 | 18 | 287 | hypothetical protein LOC100280207 [Zea mays] |
| RefSeq | XP_001702446.1 | 0 | 101 | 299 | 2 | 202 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001702447.1 | 0 | 67 | 304 | 1 | 229 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001702447.1 | 0 | 407 | 500 | 228 | 321 | carboxyesterase-related protein [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1c7i_A | 0.000000003 | 122 | 232 | 69 | 192 | A Chain A, Thermophylic Pnb Esterase |
| PDB | 1c7j_A | 0.000000003 | 122 | 232 | 69 | 192 | A Chain A, Pnb Esterase 56c8 |
| PDB | 1qe3_A | 0.000000003 | 122 | 232 | 69 | 192 | A Chain A, Pnb Esterase |
| PDB | 1akn_A | 0.000000009 | 119 | 240 | 69 | 205 | A Chain A, Structure Of Bile-salt Activated Lipase |
| PDB | 1aql_B | 0.00000001 | 119 | 240 | 69 | 205 | A Chain A, Crystal Structure Of Bovine Bile-Salt Activated Lipase Complexed With Taurocholate |
