| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; F0040; | |||||||||||
| CAZyme ID | MGYG000003301_01026 | |||||||||||
| CAZy Family | CE3 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 202; End: 2262 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE3 | 23 | 210 | 4.6e-17 | 0.979381443298969 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd01827 | sialate_O-acetylesterase_like1 | 6.20e-78 | 23 | 214 | 1 | 188 | 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. |
| pfam13472 | Lipase_GDSL_2 | 4.27e-29 | 27 | 204 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd00229 | SGNH_hydrolase | 8.26e-25 | 25 | 207 | 1 | 182 | 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. |
| pfam03629 | SASA | 1.40e-20 | 301 | 578 | 1 | 226 | Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665. |
| cd01834 | SGNH_hydrolase_like_2 | 1.61e-19 | 23 | 208 | 2 | 187 | 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 |
|---|---|---|---|---|---|
| QUB42485.1 | 2.22e-237 | 23 | 685 | 31 | 695 |
| AHW60353.1 | 2.12e-201 | 23 | 684 | 36 | 702 |
| QDT62262.1 | 5.53e-80 | 203 | 686 | 930 | 1442 |
| AWI09525.1 | 5.81e-76 | 220 | 684 | 636 | 1124 |
| QUT73831.1 | 2.08e-56 | 210 | 678 | 14 | 466 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7KMM_A | 4.12e-47 | 222 | 682 | 25 | 631 | ChainA, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306],7KMM_B Chain B, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D5EV35 | 6.94e-28 | 15 | 213 | 266 | 479 | Acetylxylan esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axeA1 PE=1 SV=1 |
| Q5RFU0 | 4.79e-24 | 219 | 572 | 25 | 388 | Sialate O-acetylesterase OS=Pongo abelii OX=9601 GN=SIAE PE=2 SV=1 |
| Q9HAT2 | 6.39e-24 | 219 | 572 | 25 | 388 | Sialate O-acetylesterase OS=Homo sapiens OX=9606 GN=SIAE PE=1 SV=1 |
| P82450 | 2.28e-23 | 204 | 572 | 14 | 415 | Sialate O-acetylesterase OS=Rattus norvegicus OX=10116 GN=Siae PE=1 SV=2 |
| P70665 | 9.33e-22 | 204 | 572 | 14 | 414 | Sialate O-acetylesterase OS=Mus musculus OX=10090 GN=Siae PE=1 SV=3 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.005717 | 0.986501 | 0.006991 | 0.000249 | 0.000249 | 0.000268 |
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