Species | Ruminococcus_F champanellensis | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_F; Ruminococcus_F champanellensis | |||||||||||
CAZyme ID | MGYG000001375_01187 | |||||||||||
CAZy Family | CE3 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1354655; End: 1355968 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 228 | 367 | 9e-18 | 0.7319587628865979 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd01834 | SGNH_hydrolase_like_2 | 3.45e-20 | 191 | 366 | 2 | 190 | 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. |
pfam13472 | Lipase_GDSL_2 | 1.66e-17 | 195 | 358 | 1 | 175 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd14256 | Dockerin_I | 1.24e-15 | 382 | 434 | 2 | 56 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
cd00229 | SGNH_hydrolase | 2.61e-15 | 193 | 371 | 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. |
COG2755 | TesA | 4.55e-15 | 190 | 379 | 8 | 215 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL17359.1 | 0.0 | 1 | 437 | 1 | 437 |
ADU20874.1 | 4.09e-127 | 26 | 373 | 478 | 820 |
BAV13051.1 | 9.76e-113 | 39 | 421 | 54 | 426 |
ADL52279.1 | 9.76e-113 | 39 | 421 | 54 | 426 |
BBH92959.1 | 6.85e-32 | 37 | 368 | 236 | 575 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.056567 | 0.860260 | 0.075526 | 0.006100 | 0.001101 | 0.000407 |
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