Species | Victivallis vadensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis | |||||||||||
CAZyme ID | MGYG000002473_01447 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 12402; End: 13439 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 25 | 240 | 1.5e-23 | 0.6754385964912281 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 3.23e-27 | 21 | 320 | 18 | 321 | 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 | 1.12e-19 | 27 | 252 | 1 | 227 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
pfam13088 | BNR_2 | 0.001 | 25 | 184 | 120 | 264 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
cd15482 | Sialidase_non-viral | 0.008 | 5 | 91 | 226 | 320 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM44758.1 | 2.55e-184 | 3 | 345 | 2 | 345 |
AYB46154.1 | 1.28e-139 | 1 | 345 | 1 | 342 |
ANY72719.1 | 2.67e-139 | 1 | 345 | 1 | 342 |
AHF91127.1 | 3.15e-127 | 3 | 345 | 2 | 357 |
AHF89372.1 | 5.80e-88 | 3 | 345 | 2 | 353 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2BF6_A | 9.39e-07 | 108 | 252 | 189 | 365 | AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens] |
2VK5_A | 9.43e-07 | 108 | 252 | 189 | 365 | 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] |
5TSP_A | 9.54e-07 | 108 | 252 | 190 | 366 | 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 |
---|---|---|---|---|---|
1.000042 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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