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CAZyme Information: MGYG000002227_01489
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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 | Eubacterium_R sp900546785 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900546785 | |||||||||||
| CAZyme ID | MGYG000002227_01489 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | Sialidase A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 20675; End: 21982 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 6 | 424 | 4.5e-90 | 0.9736842105263158 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 6.45e-93 | 5 | 425 | 2 | 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 | 1.76e-22 | 135 | 408 | 20 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| COG4409 | NanH | 5.29e-16 | 15 | 413 | 272 | 702 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13859 | BNR_3 | 7.08e-04 | 20 | 262 | 1 | 165 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| cd00260 | Sialidase | 8.36e-04 | 185 | 390 | 111 | 312 | 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 | 7.27e-114 | 5 | 432 | 39 | 471 |
| SQI63205.1 | 2.65e-110 | 1 | 430 | 4 | 445 |
| QJA08933.1 | 8.43e-88 | 6 | 430 | 246 | 680 |
| AKK05320.1 | 1.15e-82 | 4 | 429 | 331 | 762 |
| ATD57534.1 | 1.35e-81 | 15 | 430 | 396 | 830 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5TSP_A | 1.71e-82 | 15 | 430 | 21 | 448 | 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 | 3.44e-82 | 15 | 430 | 20 | 447 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 3.74e-82 | 15 | 430 | 20 | 447 | 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] |
| 2W20_A | 8.37e-66 | 8 | 411 | 16 | 448 | 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 | 9.67e-66 | 8 | 411 | 20 | 452 | 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 | 3.52e-82 | 6 | 430 | 384 | 827 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| P62576 | 1.15e-61 | 8 | 411 | 336 | 768 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| P62575 | 1.15e-61 | 8 | 411 | 336 | 768 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| Q27701 | 1.00e-40 | 15 | 432 | 289 | 758 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| P31206 | 4.76e-30 | 15 | 415 | 200 | 530 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
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 |
|---|---|---|---|---|---|
| 1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |