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CAZyme Information: MGYG000000809_01752
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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 | UBA1691 sp900549825 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA1691; UBA1691 sp900549825 | |||||||||||
| CAZyme ID | MGYG000000809_01752 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase B | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 14868; End: 16439 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 51 | 499 | 3.9e-92 | 0.9298245614035088 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 8.51e-89 | 51 | 499 | 4 | 326 | 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. |
| COG4409 | NanH | 6.67e-73 | 52 | 496 | 266 | 700 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13088 | BNR_2 | 5.20e-18 | 270 | 493 | 79 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13859 | BNR_3 | 5.94e-08 | 273 | 496 | 90 | 302 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ANU76745.2 | 4.66e-119 | 46 | 520 | 229 | 710 |
| QJU17595.1 | 4.66e-119 | 46 | 520 | 229 | 710 |
| ASU31741.1 | 4.66e-119 | 46 | 520 | 229 | 710 |
| QQQ95451.1 | 4.66e-119 | 46 | 520 | 229 | 710 |
| ETD19277.1 | 7.41e-114 | 46 | 497 | 241 | 694 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4X6K_A | 2.61e-117 | 50 | 497 | 8 | 457 | Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C] |
| 4X47_A | 2.87e-117 | 50 | 497 | 11 | 460 | 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] |
| 1SLI_A | 1.25e-111 | 34 | 497 | 185 | 650 | LeechIntramolecular Trans-Sialidase Complexed With Dana [Macrobdella decora],1SLL_A Sialidase L From Leech Macrobdella Decora [Macrobdella decora],2SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac, The Reaction Product [Macrobdella decora],3SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac Prepared By Soaking With 3'-Sialyllactose [Macrobdella decora],4SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2- Propenyl-Neu5ac, An Inactive Substrate Analogue [Macrobdella decora] |
| 5TSP_A | 1.70e-95 | 41 | 496 | 5 | 430 | Crystalstructure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124],5TSP_B Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124] |
| 2BF6_A | 2.37e-95 | 41 | 496 | 4 | 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 |
|---|---|---|---|---|---|---|
| Q27701 | 5.50e-110 | 34 | 497 | 265 | 730 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| P29767 | 1.08e-88 | 41 | 502 | 376 | 815 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| Q54727 | 3.05e-80 | 50 | 497 | 233 | 670 | Sialidase B OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=nanB PE=1 SV=2 |
| P62576 | 7.34e-60 | 34 | 517 | 314 | 789 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| P62575 | 7.34e-60 | 34 | 517 | 314 | 789 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.918225 | 0.072453 | 0.004037 | 0.000399 | 0.000250 | 0.004656 |
