| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s540_9V6.1 |
| Family | CE10 |
| Protein Properties | Length: 427 Molecular Weight: 46726.3 Isoelectric Point: 6.5852 |
| Chromosome | Chromosome/Scaffold: 540 Start: 35583 End: 37915 |
| 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 | 110 | 415 | 0 |
| DGHGQAHGYQGYVPSNSEKNHKKLPVMIQFHGGAFVTGSKDSSANDIFCRRMAKACNVIVIAVGYRLALEHKCPAAYEDGFEALHWLAKQANLAECSKSA TYIPAGFMYKGSDSYKELVDSFGDSALEPWIAAHGDVSRTIILGVSSGGNIADHVTRMTIRDASSIEPVKVVAQALMYPFFLGKVQTRSEIKLANTYFYD KASCLLAWKLFLPDEEFDLDHPAVNPLNSSREPLLKQMPPTLVVVAELDWMKDRAIAYAEALRKAGVDAPVLEYKDAVHEFATLDLLVKSRQAESCAEDM AIWIKK | |||
| Full Sequence |
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| Protein Sequence Length: 427 Download |
| MPGVGVKLYS VFFKFLLKQR LSNTGAPNND GYGLISLGSN VSTPANASFV DGVATKDVNI 60 DPFTSLSLRI FLPQSALPNH SRAVFLGKIE SIDESGWESN SQQLDVRPSD GHGQAHGYQG 120 YVPSNSEKNH KKLPVMIQFH GGAFVTGSKD SSANDIFCRR MAKACNVIVI AVGYRLALEH 180 KCPAAYEDGF EALHWLAKQA NLAECSKSAT YIPAGFMYKG SDSYKELVDS FGDSALEPWI 240 AAHGDVSRTI ILGVSSGGNI ADHVTRMTIR DASSIEPVKV VAQALMYPFF LGKVQTRSEI 300 KLANTYFYDK ASCLLAWKLF LPDEEFDLDH PAVNPLNSSR EPLLKQMPPT LVVVAELDWM 360 KDRAIAYAEA LRKAGVDAPV LEYKDAVHEF ATLDLLVKSR QAESCAEDMA IWIKKQIVAK 420 GTEFSY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG2272 | PnbA | 1.0e-5 | 127 | 194 | 68 | + Carboxylesterase type B [Lipid metabolism] | ||
| cd00312 | Esterase_lipase | 5.0e-7 | 121 | 176 | 56 | + 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. | ||
| pfam00135 | COesterase | 4.0e-8 | 121 | 176 | 57 | + Carboxylesterase family. | ||
| COG0657 | Aes | 5.0e-36 | 60 | 394 | 343 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-59 | 136 | 391 | 256 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| 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 | AAS99713.1 | 0 | 1 | 426 | 1 | 428 | At3g27320 [Arabidopsis thaliana] |
| RefSeq | NP_001030781.1 | 0 | 1 | 426 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_001785892.1 | 0 | 1 | 426 | 1 | 426 | GLP5 GID1-like protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002267088.1 | 0 | 1 | 426 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002267130.1 | 0 | 1 | 426 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| 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 | 3ed1_F | 1e-33 | 133 | 393 | 112 | 330 | N Chain N, Structure Of The 30s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Components Into Cryo-Em Map Emd-1056 |
| PDB | 3ed1_E | 1e-33 | 133 | 393 | 112 | 330 | N Chain N, Structure Of The 30s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Components Into Cryo-Em Map Emd-1056 |
| PDB | 3ed1_D | 1e-33 | 133 | 393 | 112 | 330 | N Chain N, Structure Of The 30s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Components Into Cryo-Em Map Emd-1056 |
| PDB | 3ed1_C | 1e-33 | 133 | 393 | 112 | 330 | N Chain N, Structure Of The 30s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Components Into Cryo-Em Map Emd-1056 |
| PDB | 3ed1_B | 1e-33 | 133 | 393 | 112 | 330 | N Chain N, Structure Of The 30s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Components Into Cryo-Em Map Emd-1056 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| FC450039 | 246 | 53 | 298 | 0 |
| GO362523 | 304 | 119 | 417 | 0 |
| FC355344 | 206 | 1 | 206 | 0 |
| FC424853 | 206 | 222 | 427 | 0 |
| ES789976 | 314 | 118 | 427 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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