Species | Paenibacillus amylolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus | |||||||||||
CAZyme ID | MGYG000003072_04109 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 76828; End: 78111 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 73 | 246 | 4.1e-38 | 0.9878787878787879 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 3.37e-16 | 71 | 253 | 1 | 184 | 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. |
pfam13472 | Lipase_GDSL_2 | 1.07e-12 | 74 | 248 | 2 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd01834 | SGNH_hydrolase_like_2 | 4.71e-10 | 70 | 250 | 3 | 185 | 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. |
cd01827 | sialate_O-acetylesterase_like1 | 1.41e-06 | 69 | 250 | 1 | 180 | sialate O-acetylesterase_like family of the SGNH hydrolases, 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. |
cd01831 | Endoglucanase_E_like | 0.005 | 71 | 253 | 2 | 164 | Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QYK61360.1 | 4.15e-184 | 19 | 426 | 174 | 579 |
QSF46877.1 | 5.91e-166 | 19 | 425 | 173 | 577 |
ADU21606.1 | 5.72e-36 | 36 | 426 | 635 | 981 |
EEV02614.1 | 5.48e-33 | 39 | 282 | 3 | 235 |
BCJ92770.1 | 8.62e-33 | 39 | 346 | 3 | 288 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 2.24e-34 | 39 | 282 | 3 | 235 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82] |
6HFZ_A | 4.28e-34 | 39 | 282 | 3 | 235 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000066 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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