| Species | Ruminococcus_C sp000437175 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000437175 | |||||||||||
| CAZyme ID | MGYG000004275_01526 | |||||||||||
| CAZy Family | CE3 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1523; End: 3493 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE3 | 40 | 278 | 2.2e-42 | 0.9896907216494846 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd01833 | XynB_like | 3.37e-35 | 40 | 277 | 1 | 155 | SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are 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 Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| pfam00657 | Lipase_GDSL | 1.45e-17 | 42 | 275 | 1 | 224 | GDSL-like Lipase/Acylhydrolase. |
| pfam13472 | Lipase_GDSL_2 | 6.18e-16 | 44 | 270 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd00229 | SGNH_hydrolase | 3.00e-11 | 42 | 278 | 1 | 187 | 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. |
| cd01834 | SGNH_hydrolase_like_2 | 3.01e-10 | 41 | 276 | 3 | 189 | SGNH_hydrolase subfamily. SGNH hydrolases are 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 Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAB55348.1 | 4.76e-48 | 30 | 300 | 34 | 280 |
| AWI67000.1 | 7.94e-38 | 40 | 279 | 98 | 314 |
| AAQ10005.1 | 1.64e-34 | 36 | 279 | 40 | 259 |
| AAQ10006.1 | 1.64e-34 | 36 | 279 | 40 | 259 |
| CAA84537.1 | 2.17e-32 | 31 | 279 | 428 | 655 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2VPT_A | 3.16e-18 | 37 | 275 | 3 | 191 | ChainA, LIPOLYTIC ENZYME [Acetivibrio thermocellus] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9RLB8 | 9.52e-49 | 30 | 300 | 34 | 280 | Multidomain esterase OS=Ruminococcus flavefaciens OX=1265 GN=cesA PE=1 SV=1 |
| P15329 | 1.63e-09 | 117 | 275 | 5 | 133 | Putative endoglucanase X (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celX PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000304 | 0.998951 | 0.000223 | 0.000199 | 0.000167 | 0.000139 |
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