| Species | Robinsoniella sp900540475 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475 | |||||||||||
| CAZyme ID | MGYG000001063_01658 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 10121; End: 15253 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 424 | 746 | 8.3e-79 | 0.9327485380116959 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 1.23e-80 | 424 | 753 | 6 | 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. |
| pfam13385 | Laminin_G_3 | 6.32e-26 | 906 | 1058 | 2 | 150 | Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. |
| pfam13472 | Lipase_GDSL_2 | 2.86e-25 | 1185 | 1372 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| pfam13088 | BNR_2 | 2.59e-24 | 443 | 726 | 1 | 272 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00229 | SGNH_hydrolase | 7.21e-23 | 1185 | 1380 | 3 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QEC45249.1 | 3.41e-76 | 426 | 766 | 39 | 388 |
| ATP57352.1 | 1.54e-75 | 403 | 757 | 21 | 382 |
| QIF01538.1 | 9.49e-75 | 422 | 757 | 32 | 398 |
| QDT56755.1 | 3.15e-74 | 422 | 757 | 31 | 397 |
| QOV89244.1 | 3.33e-72 | 420 | 758 | 28 | 388 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1EUR_A | 3.83e-37 | 418 | 757 | 10 | 359 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 1EUT_A | 1.96e-35 | 418 | 757 | 10 | 359 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
| 2BZD_A | 3.35e-35 | 418 | 757 | 6 | 355 | Galactoserecognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_B Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_C Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens] |
| 1WCQ_A | 5.98e-35 | 418 | 757 | 6 | 355 | Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens] |
| 1W8N_A | 1.42e-34 | 418 | 757 | 6 | 355 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q02834 | 1.64e-34 | 418 | 757 | 52 | 401 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
| P31206 | 2.43e-31 | 425 | 742 | 195 | 528 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
| P29767 | 2.97e-25 | 402 | 782 | 371 | 851 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| A5PF10 | 1.71e-21 | 432 | 740 | 78 | 395 | Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 SV=1 |
| O35657 | 9.08e-21 | 432 | 713 | 71 | 355 | Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.059700 | 0.189852 | 0.747393 | 0.001186 | 0.000969 | 0.000894 |
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