| Basic Information | |
|---|---|
| Species | Phaseolus vulgaris |
| Cazyme ID | Phvul.008G149400.1 |
| Family | CE10 |
| Protein Properties | Length: 463 Molecular Weight: 50446.4 Isoelectric Point: 8.0318 |
| Chromosome | Chromosome/Scaffold: 08 Start: 30486972 End: 30490730 |
| 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 | 25 | 452 | 0 |
| IQTSSQHSDPFGITTRPEESVAAANPSFADGVATKDIHIDPLTSLSIRIFLPESALTAPELHSKPNNRPNHEPQPQPRSARLDSIARRKSYGPPLLEERR SNSCGGGSSVEGLNLMTDGAYRGYSPPAGAKGERRRLPVVLQFHGGGWVSGGSDSAANDVFCRRITELCDVIVIAVGYRLAPENRYPAAFEDGVKVLNWL AKQANLAECSRSMGGGRSGGHGGGNGGGEFKKSDAHKHIVDSFGASVVEPWLAAHADPSRCVLLGSSCGANIADYVARKAVEGGKLLDPVKVVAQVLMYP FFVGSVPTRSEIKLANSYFYDKAMCTLSWKLFLPEEEFSLDHPAANPLVPDRGPPLKLMPPTLTVVAEHDWMRDRAIAYSEELRKVNVDAPVLEYKDAVH EFATLDVLLKSPQAQVCAEDIAIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 463 Download |
| MPSVAVKLYS VFFKFLLKHR LQNRIQTSSQ HSDPFGITTR PEESVAAANP SFADGVATKD 60 IHIDPLTSLS IRIFLPESAL TAPELHSKPN NRPNHEPQPQ PRSARLDSIA RRKSYGPPLL 120 EERRSNSCGG GSSVEGLNLM TDGAYRGYSP PAGAKGERRR LPVVLQFHGG GWVSGGSDSA 180 ANDVFCRRIT ELCDVIVIAV GYRLAPENRY PAAFEDGVKV LNWLAKQANL AECSRSMGGG 240 RSGGHGGGNG GGEFKKSDAH KHIVDSFGAS VVEPWLAAHA DPSRCVLLGS SCGANIADYV 300 ARKAVEGGKL LDPVKVVAQV LMYPFFVGSV PTRSEIKLAN SYFYDKAMCT LSWKLFLPEE 360 EFSLDHPAAN PLVPDRGPPL KLMPPTLTVV AEHDWMRDRA IAYSEELRKV NVDAPVLEYK 420 DAVHEFATLD VLLKSPQAQV CAEDIAIWVK KYISLRGHEF SY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00135 | COesterase | 2.0e-5 | 151 | 206 | 59 | + Carboxylesterase family. | ||
| cd00312 | Esterase_lipase | 9.0e-6 | 151 | 226 | 85 | + 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 | 1.0e-7 | 95 | 229 | 140 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 1.0e-33 | 145 | 446 | 303 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 2.0e-60 | 164 | 427 | 264 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAS99713.1 | 0 | 1 | 462 | 1 | 428 | At3g27320 [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 462 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002267088.1 | 0 | 1 | 462 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002267130.1 | 0 | 1 | 462 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 462 | 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 | 3e-32 | 161 | 429 | 113 | 331 | A Chain A, The Crystal Structure Of Mouse Exo70 Reveals Unique Features Of The Mammalian Exocyst |
| PDB | 2zsh_A | 3e-32 | 161 | 429 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 2e-28 | 161 | 429 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 2e-28 | 161 | 429 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 2e-28 | 161 | 429 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| ES789976 | 383 | 90 | 463 | 0 |
| HO792077 | 282 | 43 | 324 | 0 |
| EB438845 | 285 | 179 | 463 | 0 |
| JK515504 | 274 | 190 | 463 | 0 |
| DR937200 | 279 | 185 | 463 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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