| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G47480.1 |
| Family | CE10 |
| Protein Properties | Length: 315 Molecular Weight: 35255.4 Isoelectric Point: 4.983 |
| Chromosome | Chromosome/Scaffold: 1 Start: 17417579 End: 17419432 |
| Description | gibberellin receptor GID1L2, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 37 | 310 | 0 |
| LDPITGVFSKDIIIEPKTGLSARIYRPFSIQPGQKIPLMLYFHGGAFLISSTSFPSYHTSLNKIVNQANVIAVSVNYRLAPEHPLPTAYEDSWTALKNIQ AINEPWINDYADLDSLFLVGDSAGANISHHLAFRAKQSDQTLKIKGIGMIHPYFWGTQPIGAEIKDEARKQMVDGWWEFVCPSEKGSDDPWINPFADGSP DLGGLGCERVMITVAEKDILNERGKMYYERLVKSEWKGKVEIMETKEKDHVFHIFEPDCDEAMEMVRCLALFIN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 315 Download |
| MESTKKQVSL ELLPWLVVHT DGTVERLAGT EVCPPGLDPI TGVFSKDIII EPKTGLSARI 60 YRPFSIQPGQ KIPLMLYFHG GAFLISSTSF PSYHTSLNKI VNQANVIAVS VNYRLAPEHP 120 LPTAYEDSWT ALKNIQAINE PWINDYADLD SLFLVGDSAG ANISHHLAFR AKQSDQTLKI 180 KGIGMIHPYF WGTQPIGAEI KDEARKQMVD GWWEFVCPSE KGSDDPWINP FADGSPDLGG 240 LGCERVMITV AEKDILNERG KMYYERLVKS EWKGKVEIME TKEKDHVFHI FEPDCDEAME 300 MVRCLALFIN QVEA* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00135 | COesterase | 2.0e-7 | 60 | 117 | 58 | + Carboxylesterase family. | ||
| COG2272 | PnbA | 4.0e-8 | 31 | 161 | 142 | + Carboxylesterase type B [Lipid metabolism] | ||
| cd00312 | Esterase_lipase | 2.0e-9 | 60 | 167 | 121 | + 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. | ||
| COG0657 | Aes | 3.0e-27 | 33 | 294 | 271 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 4.0e-57 | 75 | 290 | 221 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005575 | cellular_component |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAM61103.1 | 0 | 1 | 314 | 1 | 314 | unknown [Arabidopsis thaliana] |
| GenBank | ABB89003.1 | 0 | 3 | 311 | 4 | 315 | CXE carboxylesterase [Malus pumila] |
| RefSeq | NP_564507.1 | 0 | 1 | 314 | 1 | 314 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002510251.1 | 0 | 3 | 311 | 2 | 311 | Gibberellin receptor GID1, putative [Ricinus communis] |
| RefSeq | XP_002526230.1 | 0 | 1 | 311 | 1 | 319 | catalytic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ed1_F | 2e-37 | 16 | 310 | 32 | 348 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 3ed1_E | 2e-37 | 16 | 310 | 32 | 348 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 3ed1_D | 2e-37 | 16 | 310 | 32 | 348 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 3ed1_C | 2e-37 | 16 | 310 | 32 | 348 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 3ed1_B | 2e-37 | 16 | 310 | 32 | 348 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| formononetin biosynthesis | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis I | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis II | RXN-3303 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EW737450 | 246 | 70 | 315 | 0 |
| EE539191 | 248 | 1 | 248 | 0 |
| FD949941 | 253 | 1 | 253 | 0 |
| FD945520 | 228 | 88 | 315 | 0 |
| EX017970 | 224 | 3 | 226 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
