Species | CAG-590 sp900548855 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-590; CAG-590 sp900548855 | |||||||||||
CAZyme ID | MGYG000001797_03216 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1969; End: 3099 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 40 | 349 | 6.6e-40 | 0.9210526315789473 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 9.33e-60 | 41 | 347 | 16 | 329 | 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 | 7.99e-38 | 50 | 338 | 1 | 280 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
COG3507 | XynB2 | 8.50e-05 | 50 | 140 | 101 | 187 | Beta-xylosidase [Carbohydrate transport and metabolism]. |
COG4692 | COG4692 | 9.97e-05 | 48 | 344 | 42 | 363 | Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
pfam04616 | Glyco_hydro_43 | 4.58e-04 | 45 | 115 | 71 | 133 | Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDU15387.1 | 1.41e-113 | 8 | 374 | 24 | 387 |
QDV18612.1 | 2.34e-113 | 13 | 359 | 31 | 370 |
QDT97307.1 | 6.24e-113 | 8 | 359 | 27 | 371 |
QEG17440.1 | 8.02e-113 | 8 | 374 | 24 | 387 |
QDT79764.1 | 1.14e-112 | 8 | 374 | 24 | 387 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4FJ6_A | 3.79e-06 | 135 | 341 | 299 | 504 | Crystalstructure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_B Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_C Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503],4FJ6_D Crystal structure of a glycoside hydrolase family 33, candidate sialidase (BDI_2946) from Parabacteroides distasonis ATCC 8503 at 1.90 A resolution [Parabacteroides distasonis ATCC 8503] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000035 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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