You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001420_02565
You are here: Home > Sequence: MGYG000001420_02565
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 | Alistipes senegalensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes senegalensis | |||||||||||
| CAZyme ID | MGYG000001420_02565 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 971599; End: 972762 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 33 | 381 | 1.5e-97 | 0.9766081871345029 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 2.37e-114 | 34 | 382 | 1 | 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 | 1.23e-31 | 58 | 363 | 1 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13859 | BNR_3 | 1.06e-11 | 58 | 277 | 9 | 208 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00260 | Sialidase | 1.56e-06 | 41 | 203 | 9 | 161 | 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. |
| COG4409 | NanH | 1.22e-05 | 25 | 95 | 255 | 324 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQL50302.1 | 2.06e-120 | 1 | 376 | 1 | 367 |
| AYQ36531.1 | 2.92e-120 | 1 | 378 | 3 | 362 |
| QEC45250.1 | 2.97e-114 | 25 | 378 | 87 | 430 |
| QDT97753.1 | 6.43e-113 | 6 | 378 | 9 | 373 |
| CAZ95099.1 | 2.67e-112 | 3 | 384 | 12 | 380 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6MYV_A | 3.36e-40 | 40 | 369 | 174 | 507 | Sialidase26co-crystallized with DANA-Gc [bacterium],6MYV_B Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_C Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_D Sialidase26 co-crystallized with DANA-Gc [bacterium] |
| 6MRV_A | 4.71e-40 | 40 | 369 | 195 | 528 | Sialidase26co-crystallized with DANA [bacterium],6MRV_B Sialidase26 co-crystallized with DANA [bacterium],6MRX_A Sialidase26 apo [bacterium],6MRX_B Sialidase26 apo [bacterium],6MRX_C Sialidase26 apo [bacterium],6MRX_D Sialidase26 apo [bacterium] |
| 6MNJ_A | 1.18e-39 | 40 | 369 | 193 | 524 | Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes] |
| 1EUR_A | 1.55e-39 | 25 | 381 | 2 | 359 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
| 2BF6_A | 1.42e-38 | 36 | 366 | 12 | 429 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P31206 | 7.92e-38 | 40 | 369 | 196 | 529 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
| Q02834 | 3.79e-37 | 25 | 381 | 44 | 401 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
| O35657 | 1.97e-35 | 45 | 376 | 69 | 398 | Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1 |
| Q99PW3 | 2.73e-35 | 45 | 376 | 69 | 398 | Sialidase-1 OS=Rattus norvegicus OX=10116 GN=Neu1 PE=1 SV=1 |
| A6BMK7 | 2.95e-34 | 45 | 376 | 75 | 404 | Sialidase-1 OS=Bos taurus OX=9913 GN=NEU1 PE=2 SV=2 |
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 |
|---|---|---|---|---|---|
| 0.000317 | 0.998956 | 0.000213 | 0.000170 | 0.000162 | 0.000149 |