Species | Clostridium sp900759995 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900759995 | |||||||||||
CAZyme ID | MGYG000004230_01165 | |||||||||||
CAZy Family | CBM40 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 12943; End: 17496 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 1025 | 1309 | 9.1e-124 | 0.9963503649635036 |
GH33 | 248 | 740 | 4.4e-80 | 0.9385964912280702 |
CBM40 | 59 | 232 | 6.2e-26 | 0.9385474860335196 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08023 | GH16_laminarinase_like | 7.56e-70 | 1025 | 1310 | 1 | 234 | Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. |
cd15482 | Sialidase_non-viral | 2.53e-60 | 246 | 740 | 3 | 330 | 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. |
cd00413 | Glyco_hydrolase_16 | 2.01e-27 | 1027 | 1309 | 1 | 208 | glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues. |
cd08024 | GH16_CCF | 8.36e-26 | 1025 | 1286 | 3 | 276 | Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members. |
cd02182 | GH16_Strep_laminarinase_like | 1.39e-25 | 1025 | 1291 | 6 | 237 | Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGM92253.1 | 1.00e-172 | 42 | 890 | 858 | 1693 |
ANU71609.1 | 2.55e-172 | 42 | 886 | 858 | 1689 |
ASU26373.1 | 2.55e-172 | 42 | 886 | 858 | 1689 |
QQR10962.1 | 2.55e-172 | 42 | 886 | 858 | 1689 |
ARV02485.1 | 2.55e-172 | 42 | 886 | 858 | 1689 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2W20_A | 6.67e-72 | 250 | 733 | 19 | 448 | Structureof the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6],2W20_B Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6] |
3H72_A | 7.83e-72 | 250 | 733 | 23 | 452 | Crystalstructure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H72_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H73_A Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6],3H73_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6] |
7A54_A | 1.36e-71 | 250 | 733 | 46 | 475 | ChainA, Sialidase A [Streptococcus pneumoniae],7A54_B Chain B, Sialidase A [Streptococcus pneumoniae],7A5X_A Chain A, Sialidase A [Streptococcus pneumoniae],7A5X_B Chain B, Sialidase A [Streptococcus pneumoniae] |
2VVZ_A | 1.58e-71 | 250 | 733 | 21 | 450 | Structureof the catalytic domain of Streptococcus pneumoniae sialidase NanA [Streptococcus pneumoniae],2VVZ_B Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA [Streptococcus pneumoniae] |
2YA4_A | 2.19e-71 | 250 | 733 | 40 | 469 | Crystalstructure of Streptococcus pneumoniae NanA (TIGR4) [Streptococcus pneumoniae TIGR4],2YA4_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) [Streptococcus pneumoniae TIGR4],2YA5_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with sialic acid [Streptococcus pneumoniae TIGR4],2YA5_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with sialic acid [Streptococcus pneumoniae TIGR4],2YA6_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with DANA [Streptococcus pneumoniae TIGR4],2YA6_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with DANA [Streptococcus pneumoniae TIGR4],2YA7_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_C Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA7_D Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Zanamivir [Streptococcus pneumoniae TIGR4],2YA8_A Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Oseltamivir carboxylate [Streptococcus pneumoniae TIGR4],2YA8_B Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with Oseltamivir carboxylate [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P62575 | 2.62e-69 | 66 | 842 | 139 | 868 | Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1 |
P62576 | 2.62e-69 | 66 | 842 | 139 | 868 | Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1 |
P29767 | 5.10e-66 | 57 | 898 | 200 | 991 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
P23903 | 1.02e-33 | 1025 | 1309 | 427 | 677 | Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1 |
Q27701 | 9.11e-33 | 36 | 748 | 73 | 739 | Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000406 | 0.998061 | 0.000992 | 0.000194 | 0.000166 | 0.000140 |
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