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CAZyme Information: MGYG000003156_01120
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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 sp900544515 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900544515 | |||||||||||
| CAZyme ID | MGYG000003156_01120 | |||||||||||
| CAZy Family | GH33 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2224; End: 7842 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH33 | 52 | 496 | 6.1e-59 | 0.9327485380116959 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 3.19e-37 | 51 | 491 | 9 | 332 | 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 | 5.63e-16 | 23 | 483 | 239 | 701 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
| pfam13088 | BNR_2 | 6.00e-05 | 224 | 369 | 66 | 200 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam13088 | BNR_2 | 0.006 | 244 | 341 | 191 | 278 | 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 |
|---|---|---|---|---|---|
| ANU47084.1 | 7.69e-53 | 20 | 490 | 1184 | 1667 |
| QQQ98205.1 | 7.69e-53 | 20 | 490 | 1184 | 1667 |
| ARE59829.1 | 1.39e-45 | 14 | 482 | 10 | 490 |
| QQR06511.1 | 1.39e-45 | 14 | 482 | 10 | 490 |
| QJA08933.1 | 7.75e-37 | 53 | 484 | 254 | 664 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4X6K_A | 5.53e-37 | 53 | 482 | 16 | 456 | Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C] |
| 4X47_A | 5.81e-37 | 53 | 482 | 19 | 459 | 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] |
| 5TSP_A | 1.11e-33 | 38 | 484 | 2 | 432 | 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 | 2.21e-33 | 38 | 484 | 1 | 431 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
| 2VK5_A | 2.33e-33 | 38 | 484 | 1 | 431 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P29767 | 8.37e-35 | 30 | 482 | 362 | 809 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
| Q27701 | 1.90e-30 | 53 | 482 | 289 | 729 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
| P62575 | 5.22e-24 | 55 | 482 | 345 | 768 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
| P62576 | 5.22e-24 | 55 | 482 | 345 | 768 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
| P15698 | 1.16e-08 | 20 | 495 | 10 | 392 | Sialidase OS=Paeniclostridium sordellii OX=1505 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 |
|---|---|---|---|---|---|
| 0.000410 | 0.998740 | 0.000226 | 0.000229 | 0.000189 | 0.000157 |
