| Species | Paenibacillus_A sp900069005 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005 | |||||||||||
| CAZyme ID | MGYG000001542_02358 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 47338; End: 48450 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 25 | 307 | 1.1e-39 | 0.8304093567251462 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 2.27e-46 | 25 | 305 | 18 | 303 | 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 | 4.72e-32 | 32 | 308 | 1 | 265 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd15482 | Sialidase_non-viral | 2.58e-12 | 12 | 157 | 188 | 320 | 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. |
| pfam13859 | BNR_3 | 8.63e-07 | 46 | 235 | 20 | 211 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AZS16817.1 | 4.40e-262 | 1 | 370 | 20 | 389 |
| QDS98808.1 | 1.44e-107 | 3 | 359 | 397 | 745 |
| APZ92631.1 | 6.16e-48 | 18 | 302 | 306 | 582 |
| QDT48634.1 | 6.59e-47 | 14 | 330 | 306 | 619 |
| QDT79793.1 | 1.23e-46 | 14 | 325 | 303 | 611 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4X6K_A | 3.54e-06 | 118 | 236 | 240 | 357 | Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C] |
| 4X47_A | 3.55e-06 | 118 | 236 | 243 | 360 | Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en [[Ruminococcus] gnavus ATCC 29149],4X49_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with oseltamivir carboxylate [[Ruminococcus] gnavus ATCC 29149],4X4A_A Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac [[Ruminococcus] gnavus ATCC 29149] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000030 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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