Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 35861.m000015 |
Family | CE12 |
Protein Properties | Length: 414 Molecular Weight: 44640.3 Isoelectric Point: 9.4341 |
Chromosome | Chromosome/Scaffold: 35861 Start: 76 End: 1319 |
Description | |
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 |
CE12 | 327 | 405 | 3.2e-32 |
TLYLVGDSTVKSGGVNGAIGWGERIAPYFDARKINVVNAAIGGRSSRTYFTEGRWDKVRDQLKRGDVVLIQFGHNDGGR | |||
CE12 | 52 | 277 | 0 |
LILIGDSTVRNGRDDGQGKGVAGQWGWGNPVAAWFDPAKVNVVNRAVGGLSSRTYITSGHWERTLAFVKRGDIVVMQFGHNDAGAVNDASRARGTLHGTG NETEEIDNLLTHRHETVHTYGWYLRKYVADIRAKGATPVICSPIPHKQWDAAGRAKRDRDTYGGWAAAVAKAEGVGFIDLNEGIARRYDALGHDAVVQLF PQTTPDEHTHTNWAGAVLNAQVAVEG |
Full Sequence |
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Protein Sequence Length: 414 Download |
MPLLSTLLRT VALVVLTVAG VHAQPLPAAV NTDPARAQVS LPEPANPALP SLILIGDSTV 60 RNGRDDGQGK GVAGQWGWGN PVAAWFDPAK VNVVNRAVGG LSSRTYITSG HWERTLAFVK 120 RGDIVVMQFG HNDAGAVNDA SRARGTLHGT GNETEEIDNL LTHRHETVHT YGWYLRKYVA 180 DIRAKGATPV ICSPIPHKQW DAAGRAKRDR DTYGGWAAAV AKAEGVGFID LNEGIARRYD 240 ALGHDAVVQL FPQTTPDEHT HTNWAGAVLN AQVAVEGMKA LGDPRIAAWL KARAPVDLQP 300 PAREDDRPVV DARSVRDEAP RDATLPTLYL VGDSTVKSGG VNGAIGWGER IAPYFDARKI 360 NVVNAAIGGR SSRTYFTEGR WDKVRDQLKR GDVVLIQFGH NDGGRIGDPA MKNR 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13472 | Lipase_GDSL_2 | 2.0e-6 | 331 | 405 | 75 | + GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. | ||
COG2755 | TesA | 7.0e-11 | 321 | 404 | 88 | + Lysophospholipase L1 and related esterases [Amino acid transport and metabolism] | ||
pfam13472 | Lipase_GDSL_2 | 5.0e-11 | 53 | 267 | 215 | + GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. | ||
cd01821 | Rhamnogalacturan_acetylesterase_like | 1.0e-29 | 326 | 408 | 84 | + Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria. | ||
cd01821 | Rhamnogalacturan_acetylesterase_like | 1.0e-60 | 50 | 278 | 229 | + Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria. |
Gene Ontology | |
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GO Term | Description |
GO:0006629 | lipid metabolic process |
GO:0016788 | hydrolase activity, acting on ester bonds |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002537810.1 | 0 | 1 | 414 | 1 | 414 | conserved hypothetical protein [Ricinus communis] |
RefSeq | YP_001818241.1 | 0 | 1 | 408 | 6 | 403 | GDSL family lipase [Opitutus terrae PB90-1] |
RefSeq | YP_001818241.1 | 0 | 39 | 292 | 307 | 551 | GDSL family lipase [Opitutus terrae PB90-1] |
RefSeq | ZP_01061984.1 | 0 | 1 | 412 | 1 | 357 | putative rhamnogalacturonan acetylesterase [Leeuwenhoekiella blandensis MED217] |
RefSeq | ZP_01061984.1 | 0 | 42 | 290 | 263 | 497 | putative rhamnogalacturonan acetylesterase [Leeuwenhoekiella blandensis MED217] |
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 | 1pp4_B | 1e-16 | 93 | 282 | 35 | 216 | A Chain A, Structure Of The Retaining Glycosyltransferase Msha: The First Step In Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum- Apo (Open) Structure. |
PDB | 1pp4_B | 0.000000000003 | 327 | 406 | 2 | 79 | A Chain A, Structure Of The Retaining Glycosyltransferase Msha: The First Step In Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum- Apo (Open) Structure. |
PDB | 1pp4_A | 1e-16 | 93 | 282 | 35 | 216 | A Chain A, Structure Of The Retaining Glycosyltransferase Msha: The First Step In Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum- Apo (Open) Structure. |
PDB | 1pp4_A | 0.000000000003 | 327 | 406 | 2 | 79 | A Chain A, Structure Of The Retaining Glycosyltransferase Msha: The First Step In Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum- Apo (Open) Structure. |
PDB | 1k7c_A | 1e-16 | 93 | 282 | 35 | 216 | A Chain A, Structure Of The Retaining Glycosyltransferase Msha: The First Step In Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum- Apo (Open) Structure. |
Signal Peptide | |||||
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Cleavage Site | |||||
23 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EC954499 | 232 | 51 | 278 | 2e-24 |
EX516891 | 178 | 90 | 267 | 5e-19 |
GO793442 | 247 | 51 | 292 | 1e-18 |
EC954499 | 80 | 327 | 404 | 0.00000000000002 |
EX516891 | 81 | 327 | 406 | 0.000000004 |
Orthologous Group | |||||
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Species | ID | ||||
Ricinus communis | 35861.m000015.327.405 | 35861.m000015.327.405 | 35861.m000015.52.277 | 35861.m000015.52.277 |
Sequence Alignments (This image is cropped. Click for full image.) |
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