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CAZyme Information: MGYG000001572_01149
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; | |||||||||||
| CAZyme ID | MGYG000001572_01149 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 92479; End: 93789 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 13 | 426 | 2.6e-91 | 0.956140350877193 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 4.27e-94 | 8 | 427 | 3 | 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 | 1.48e-16 | 174 | 409 | 71 | 279 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 2.29e-13 | 14 | 415 | 269 | 702 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13859 | BNR_3 | 8.49e-06 | 30 | 265 | 8 | 166 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00260 | Sialidase | 0.001 | 166 | 405 | 93 | 327 | 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 |
|---|---|---|---|---|---|
| AUS96375.1 | 9.78e-123 | 8 | 433 | 40 | 470 |
| SQI63205.1 | 9.71e-111 | 2 | 433 | 3 | 446 |
| QJA08933.1 | 9.91e-92 | 4 | 432 | 242 | 680 |
| AKK05320.1 | 1.54e-90 | 6 | 434 | 331 | 765 |
| AMN34958.1 | 1.02e-87 | 17 | 436 | 262 | 693 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5TSP_A | 7.87e-91 | 17 | 436 | 21 | 452 | 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] |
| 2VK5_A | 1.71e-90 | 17 | 436 | 20 | 451 | TheStructure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK6_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_B The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens] |
| 2BF6_A | 8.74e-90 | 17 | 433 | 20 | 448 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2W20_A | 2.34e-70 | 20 | 431 | 26 | 469 | Structureof the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6],2W20_B Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6] |
| 3H72_A | 2.72e-70 | 20 | 431 | 30 | 473 | Crystalstructure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H72_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H73_A Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6],3H73_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29767 | 1.81e-80 | 8 | 434 | 384 | 829 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| P62575 | 6.86e-66 | 20 | 431 | 346 | 789 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| P62576 | 6.86e-66 | 20 | 431 | 346 | 789 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| Q27701 | 8.65e-42 | 17 | 433 | 289 | 757 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| Q02834 | 2.11e-29 | 20 | 433 | 67 | 403 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA 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 |
|---|---|---|---|---|---|
| 1.000063 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |