Species | Prevotella timonensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella timonensis | |||||||||||
CAZyme ID | MGYG000003794_01008 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 14524; End: 15762 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 31 | 385 | 1.3e-46 | 0.9444444444444444 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 1.85e-58 | 29 | 392 | 1 | 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 | 9.48e-05 | 71 | 374 | 14 | 279 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
PRK11545 | gntK | 0.002 | 90 | 143 | 35 | 91 | gluconokinase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALO48969.1 | 4.24e-172 | 27 | 405 | 25 | 403 |
QYR10380.1 | 1.41e-141 | 19 | 401 | 17 | 395 |
EFC70822.1 | 2.43e-103 | 28 | 406 | 20 | 407 |
QFQ12979.1 | 3.31e-100 | 28 | 404 | 20 | 400 |
QUB83288.1 | 3.37e-99 | 35 | 403 | 38 | 427 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7MHU_A | 1.62e-17 | 31 | 407 | 39 | 402 | ChainA, Exo-alpha-sialidase [Bacteroides acidifaciens],7MHU_B Chain B, Exo-alpha-sialidase [Bacteroides acidifaciens] |
2BF6_A | 3.70e-11 | 31 | 394 | 12 | 444 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
2VK5_A | 3.73e-11 | 31 | 394 | 12 | 444 | 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] |
7LBU_A | 5.00e-11 | 13 | 378 | 75 | 413 | ChainA, Exo-alpha-sialidase [Cutibacterium acnes],7LBV_A Chain A, Exo-alpha-sialidase [Cutibacterium acnes] |
5TSP_A | 1.19e-10 | 31 | 394 | 13 | 445 | 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] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000297 | 0.999012 | 0.000203 | 0.000148 | 0.000141 | 0.000143 |
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