Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; | |||||||||||
CAZyme ID | MGYG000004759_01188 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | Sialidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5844; End: 7124 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 51 | 411 | 9e-48 | 0.956140350877193 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 1.04e-62 | 48 | 414 | 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. |
COG4409 | NanH | 5.07e-08 | 58 | 211 | 274 | 446 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QFQ12979.1 | 2.94e-121 | 48 | 425 | 23 | 399 |
QYR10380.1 | 5.24e-117 | 57 | 423 | 35 | 395 |
EFC70822.1 | 2.21e-113 | 48 | 426 | 23 | 405 |
ALO48969.1 | 3.92e-113 | 48 | 425 | 29 | 401 |
ANR74021.1 | 1.71e-89 | 57 | 425 | 47 | 430 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1EUR_A | 1.20e-13 | 55 | 404 | 20 | 348 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
2BF6_A | 1.31e-13 | 43 | 421 | 7 | 449 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
2VK5_A | 1.32e-13 | 43 | 421 | 7 | 449 | 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] |
1EUT_A | 2.37e-13 | 55 | 404 | 20 | 348 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
5TSP_A | 2.41e-13 | 43 | 421 | 8 | 450 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q02834 | 1.36e-12 | 55 | 404 | 62 | 390 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
P10481 | 1.31e-11 | 59 | 332 | 36 | 311 | Sialidase OS=Clostridium perfringens OX=1502 GN=nanH PE=1 SV=1 |
P31206 | 2.04e-11 | 50 | 418 | 194 | 542 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
P62575 | 4.74e-10 | 15 | 372 | 289 | 682 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
P62576 | 4.74e-10 | 15 | 372 | 289 | 682 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000252 | 0.999116 | 0.000159 | 0.000163 | 0.000149 | 0.000138 |
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