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CAZyme Information: MGYG000001512_03123
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Coprobacter secundus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus | |||||||||||
| CAZyme ID | MGYG000001512_03123 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1415432; End: 1416649 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 29 | 368 | 1.2e-88 | 0.9473684210526315 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 8.00e-99 | 30 | 374 | 2 | 335 | 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 | 3.00e-27 | 53 | 359 | 1 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 6.36e-11 | 42 | 361 | 275 | 639 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| cd00260 | Sialidase | 1.27e-07 | 34 | 386 | 7 | 358 | sialidases/neuraminidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QXD26332.1 | 1.71e-195 | 13 | 400 | 7 | 405 |
| QXD30397.1 | 1.71e-195 | 13 | 400 | 7 | 405 |
| QDU14541.1 | 4.79e-124 | 1 | 386 | 6 | 388 |
| QDT89470.1 | 6.79e-124 | 1 | 386 | 6 | 388 |
| QEG16519.1 | 1.93e-123 | 1 | 386 | 6 | 388 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1EUR_A | 2.06e-31 | 36 | 386 | 19 | 359 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 1W8N_A | 2.99e-31 | 36 | 386 | 15 | 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] |
| 2BZD_A | 2.55e-30 | 36 | 386 | 15 | 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] |
| 1EUT_A | 2.60e-30 | 36 | 386 | 19 | 359 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
| 1WCQ_A | 8.64e-30 | 36 | 386 | 15 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q99519 | 1.81e-30 | 42 | 371 | 77 | 400 | Sialidase-1 OS=Homo sapiens OX=9606 GN=NEU1 PE=1 SV=1 |
| Q5RAF4 | 1.81e-30 | 42 | 371 | 77 | 400 | Sialidase-1 OS=Pongo abelii OX=9601 GN=NEU1 PE=2 SV=1 |
| Q02834 | 1.69e-29 | 36 | 386 | 61 | 401 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
| Q99PW3 | 1.05e-28 | 42 | 364 | 71 | 390 | Sialidase-1 OS=Rattus norvegicus OX=10116 GN=Neu1 PE=1 SV=1 |
| O35657 | 1.44e-28 | 42 | 364 | 71 | 390 | Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000205 | 0.999240 | 0.000149 | 0.000142 | 0.000125 | 0.000126 |