Species | Bacteroides fragilis_A | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides fragilis_A | |||||||||||
CAZyme ID | MGYG000000236_02377 | |||||||||||
CAZy Family | CE3 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 145754; End: 147826 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 23 | 213 | 3.8e-16 | 0.9948453608247423 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd01827 | sialate_O-acetylesterase_like1 | 7.99e-83 | 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 | 3.00e-25 | 27 | 204 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd00229 | SGNH_hydrolase | 1.22e-21 | 25 | 212 | 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. |
pfam03629 | SASA | 4.62e-20 | 301 | 581 | 2 | 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 | 6.95e-16 | 23 | 212 | 2 | 191 | 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 | 1.05e-276 | 21 | 687 | 29 | 694 |
AHW60353.1 | 6.14e-231 | 18 | 690 | 31 | 705 |
AWI09525.1 | 2.64e-101 | 204 | 687 | 627 | 1124 |
QDT62262.1 | 1.15e-96 | 205 | 689 | 935 | 1442 |
QUT73831.1 | 1.56e-83 | 218 | 687 | 22 | 472 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7KMM_A | 2.49e-64 | 225 | 687 | 28 | 633 | 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 |
---|---|---|---|---|---|---|
P82450 | 1.29e-42 | 226 | 630 | 31 | 469 | Sialate O-acetylesterase OS=Rattus norvegicus OX=10116 GN=Siae PE=1 SV=2 |
P70665 | 1.11e-39 | 226 | 630 | 31 | 468 | Sialate O-acetylesterase OS=Mus musculus OX=10090 GN=Siae PE=1 SV=3 |
Q9HAT2 | 6.67e-35 | 219 | 612 | 25 | 425 | Sialate O-acetylesterase OS=Homo sapiens OX=9606 GN=SIAE PE=1 SV=1 |
Q5RFU0 | 4.05e-34 | 219 | 612 | 25 | 425 | Sialate O-acetylesterase OS=Pongo abelii OX=9601 GN=SIAE PE=2 SV=1 |
D5EV35 | 5.78e-26 | 20 | 213 | 271 | 479 | Acetylxylan esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axeA1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.024967 | 0.887782 | 0.086271 | 0.000312 | 0.000300 | 0.000355 |
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