Species | RUG572 sp900547945 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; RUG572; RUG572 sp900547945 | |||||||||||
CAZyme ID | MGYG000003483_02616 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 17358; End: 18656 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 95 | 394 | 3.5e-28 | 0.8304093567251462 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 1.98e-35 | 96 | 395 | 52 | 339 | 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 | 2.10e-24 | 74 | 375 | 1 | 278 | 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 |
---|---|---|---|---|---|
QDT83902.1 | 2.18e-108 | 43 | 425 | 44 | 411 |
QDT19814.1 | 3.09e-108 | 43 | 425 | 44 | 411 |
QGQ22401.1 | 2.47e-107 | 43 | 425 | 44 | 411 |
QEL14415.1 | 1.16e-106 | 43 | 423 | 53 | 418 |
QDU40810.1 | 1.98e-106 | 43 | 427 | 55 | 424 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1EUR_A | 3.79e-06 | 227 | 384 | 199 | 348 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
1W8N_A | 5.23e-06 | 227 | 384 | 195 | 344 | Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens] |
1EUT_A | 5.25e-06 | 227 | 384 | 199 | 348 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001064 | 0.479970 | 0.518282 | 0.000238 | 0.000230 | 0.000190 |
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