Species | Bacteroides fragilis_A | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides fragilis_A | |||||||||||
CAZyme ID | MGYG000000236_04324 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9531; End: 10631 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 6.13e-29 | 82 | 356 | 52 | 338 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
pfam13088 | BNR_2 | 3.81e-12 | 133 | 334 | 87 | 278 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
pfam13088 | BNR_2 | 1.45e-10 | 37 | 221 | 98 | 277 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
cd15482 | Sialidase_non-viral | 8.58e-09 | 155 | 291 | 17 | 176 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
cd15482 | Sialidase_non-viral | 4.15e-07 | 52 | 169 | 201 | 322 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDU73633.1 | 2.89e-113 | 26 | 364 | 204 | 544 |
QDV35524.1 | 1.85e-87 | 25 | 364 | 38 | 381 |
AQW27075.1 | 1.38e-58 | 25 | 365 | 198 | 567 |
ATD48363.1 | 1.38e-58 | 25 | 365 | 198 | 567 |
ABG82852.1 | 2.68e-58 | 25 | 365 | 198 | 567 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000219 | 0.999161 | 0.000153 | 0.000154 | 0.000134 | 0.000127 |
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