Species | Phocaeicola sp002493165 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002493165 | |||||||||||
CAZyme ID | MGYG000002171_00300 | |||||||||||
CAZy Family | CE3 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 77153; End: 79222 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE3 | 23 | 211 | 6e-16 | 0.9845360824742269 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd01827 | sialate_O-acetylesterase_like1 | 7.68e-95 | 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 | 2.66e-28 | 27 | 204 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd00229 | SGNH_hydrolase | 2.36e-23 | 25 | 211 | 1 | 186 | 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 | 2.46e-22 | 301 | 576 | 2 | 221 | 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 | 2.04e-17 | 22 | 208 | 1 | 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 | 2.93e-266 | 21 | 684 | 29 | 692 |
AHW60353.1 | 4.40e-246 | 20 | 684 | 33 | 700 |
QDT62262.1 | 3.56e-95 | 191 | 689 | 917 | 1443 |
AWI09525.1 | 5.98e-95 | 220 | 685 | 636 | 1123 |
QUT73831.1 | 2.12e-84 | 218 | 687 | 22 | 473 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7KMM_A | 1.43e-59 | 225 | 687 | 28 | 634 | 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 | 1.28e-42 | 226 | 630 | 31 | 469 | Sialate O-acetylesterase OS=Rattus norvegicus OX=10116 GN=Siae PE=1 SV=2 |
P70665 | 3.24e-40 | 226 | 630 | 31 | 468 | Sialate O-acetylesterase OS=Mus musculus OX=10090 GN=Siae PE=1 SV=3 |
Q5RFU0 | 3.23e-36 | 219 | 665 | 25 | 482 | Sialate O-acetylesterase OS=Pongo abelii OX=9601 GN=SIAE PE=2 SV=1 |
Q9HAT2 | 5.92e-36 | 219 | 665 | 25 | 482 | Sialate O-acetylesterase OS=Homo sapiens OX=9606 GN=SIAE PE=1 SV=1 |
D5EV35 | 1.33e-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 |
---|---|---|---|---|---|
0.007826 | 0.863227 | 0.128037 | 0.000301 | 0.000280 | 0.000304 |
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