Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29633.m000885 |
Family | CE10 |
Protein Properties | Length: 472 Molecular Weight: 52058.5 Isoelectric Point: 8.0334 |
Chromosome | Chromosome/Scaffold: 29633 Start: 25264 End: 29188 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 145 | 461 | 0 |
RRNSYGCTNDVVVVESLNNVVYRGYAPNVDKTKKLPIMLQFHGGGWVSGSNDSVANDFFCRRIAKLCDVVVVAVGYRLAPENKYPAAFEDGLKVLNWLGK QANLSECSKSMGTAKGAAEFKKADLARHIVDTFGASMVEPWLAAHGDPSRCVLLGVSCGANIADYVARKAVEAGKLLDPVNVVAQVLMYPFFIGSIPTHS EIKLANSYFYDKPMCMLAWKLFLPEEEFSLDHPAANPLIPGRGPPLKLMPPTLTVVAEHDWMRDRAIAYSEELRKVNVDAPVLEYKDAVHEFATLDMLLK TPQALACAEDIAIWVKK |
Full Sequence |
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Protein Sequence Length: 472 Download |
MPSVAVKLYS VFFKFLLKHR LQSRIQTPLD SSSSSSSNPF GVTTRPEESV SAPNPSFTDG 60 VATKDIHIDP FTSLTIRIFL PESALNPPEP DSKYQSKPKA KPNPNKSSNL DHLHNDNHLH 120 VIRRNSLGHT STASNTGSPS PPESRRNSYG CTNDVVVVES LNNVVYRGYA PNVDKTKKLP 180 IMLQFHGGGW VSGSNDSVAN DFFCRRIAKL CDVVVVAVGY RLAPENKYPA AFEDGLKVLN 240 WLGKQANLSE CSKSMGTAKG AAEFKKADLA RHIVDTFGAS MVEPWLAAHG DPSRCVLLGV 300 SCGANIADYV ARKAVEAGKL LDPVNVVAQV LMYPFFIGSI PTHSEIKLAN SYFYDKPMCM 360 LAWKLFLPEE EFSLDHPAAN PLIPGRGPPL KLMPPTLTVV AEHDWMRDRA IAYSEELRKV 420 NVDAPVLEYK DAVHEFATLD MLLKTPQALA CAEDIAIWVK KYISFRGHEF SY 480 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
cd00312 | Esterase_lipase | 4.0e-5 | 169 | 241 | 83 | + 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. |
PRK10162 | PRK10162 | 2.0e-6 | 186 | 247 | 62 | + acetyl esterase; Provisional |
pfam00135 | COesterase | 1.0e-6 | 169 | 224 | 60 | + Carboxylesterase family. |
COG0657 | Aes | 1.0e-36 | 166 | 440 | 275 | + Esterase/lipase [Lipid metabolism] |
pfam07859 | Abhydrolase_3 | 7.0e-62 | 182 | 437 | 256 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
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 | ABB89022.1 | 0 | 1 | 458 | 1 | 450 | CXE carboxylesterase [Actinidia deliciosa] |
RefSeq | NP_189367.1 | 0 | 1 | 472 | 1 | 460 | hydrolase [Arabidopsis thaliana] |
RefSeq | XP_002267088.1 | 0 | 1 | 472 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002267130.1 | 0 | 1 | 472 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002526925.1 | 0 | 1 | 472 | 1 | 472 | conserved hypothetical protein [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 | 2zsi_A | 1e-32 | 179 | 439 | 113 | 331 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
PDB | 2zsh_A | 1e-32 | 179 | 439 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 6e-29 | 179 | 439 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 6e-29 | 179 | 439 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 6e-29 | 179 | 439 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES789976 | 359 | 123 | 472 | 0 |
EB438845 | 278 | 197 | 472 | 0 |
JK515504 | 266 | 208 | 472 | 0 |
DR937200 | 272 | 202 | 472 | 0 |
DR937200 | 20 | 191 | 210 | 0.65 |
Sequence Alignments (This image is cropped. Click for full image.) |
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