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CAZyme Information: MGYG000001615_05061
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Eisenbergiella sp900548905 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900548905 | |||||||||||
| CAZyme ID | MGYG000001615_05061 | |||||||||||
| CAZy Family | CE12 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11130; End: 12488 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE12 | 185 | 379 | 4.1e-46 | 0.9952380952380953 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd01821 | Rhamnogalacturan_acetylesterase_like | 1.36e-60 | 184 | 379 | 1 | 198 | 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. |
| pfam13472 | Lipase_GDSL_2 | 7.38e-13 | 190 | 367 | 3 | 173 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| COG2755 | TesA | 1.44e-11 | 185 | 379 | 10 | 204 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
| cd00229 | SGNH_hydrolase | 3.48e-09 | 190 | 377 | 5 | 186 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
| pfam00657 | Lipase_GDSL | 1.66e-07 | 186 | 375 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ASA21604.1 | 6.90e-152 | 1 | 413 | 1 | 406 |
| QKS48637.1 | 9.87e-147 | 1 | 411 | 1 | 404 |
| AOZ96642.1 | 4.26e-71 | 62 | 379 | 15 | 341 |
| ADL33886.1 | 1.09e-68 | 90 | 387 | 54 | 362 |
| QNM03704.1 | 1.93e-68 | 12 | 407 | 10 | 434 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2O14_A | 6.89e-21 | 14 | 381 | 31 | 361 | X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O31523 | 1.62e-26 | 186 | 382 | 8 | 215 | Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1 |
| P42304 | 2.22e-20 | 14 | 381 | 46 | 376 | Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |