Species | CAG-617 sp900553285 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-617; CAG-617 sp900553285 | |||||||||||
CAZyme ID | MGYG000000963_00910 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3988; End: 7305 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 797 | 1029 | 4.3e-54 | 0.991304347826087 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08023 | GH16_laminarinase_like | 1.45e-64 | 796 | 1029 | 1 | 235 | 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. |
cd00413 | Glyco_hydrolase_16 | 2.63e-30 | 798 | 1029 | 1 | 210 | 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. |
cd02182 | GH16_Strep_laminarinase_like | 3.63e-26 | 792 | 1030 | 2 | 259 | 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. |
COG2273 | BglS | 2.75e-23 | 783 | 1037 | 40 | 273 | Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]. |
cd02178 | GH16_beta_agarase | 1.33e-20 | 796 | 1030 | 25 | 258 | Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QFQ12302.1 | 5.79e-196 | 1 | 801 | 5 | 797 |
QFQ13169.1 | 1.44e-122 | 504 | 1031 | 23 | 542 |
BBA29449.1 | 4.04e-83 | 790 | 1031 | 46 | 281 |
QUB75565.1 | 5.58e-83 | 791 | 1054 | 47 | 300 |
QKH89566.1 | 3.91e-82 | 790 | 1031 | 46 | 281 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6T2R_AAA | 4.68e-34 | 789 | 1030 | 26 | 262 | ChainAAA, Beta-glycosidase [Bacteroides caccae] |
4CRQ_A | 3.86e-30 | 791 | 1031 | 2 | 232 | Crystalstructure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CRQ_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CTE_A Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans],4CTE_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans] |
6JH5_A | 5.81e-29 | 792 | 1031 | 4 | 233 | Structureof Marine bacterial laminarinase [Aquimarina] |
6JHJ_A | 3.65e-28 | 792 | 1031 | 4 | 233 | Structureof Marine bacterial laminarinase mutant-E135A [Aquimarina],6JIA_A Marine bacterial laminarinase mutant E135A complex with laminaritetraose [Aquimarina sp.],6M6P_A Structure of Marine bacterial laminarinase mutant E135A in complex with 1,3-beta-cellotriosyl-glucose [Aquimarina sp.] |
3ATG_A | 1.41e-24 | 794 | 1029 | 5 | 238 | endo-1,3-beta-glucanasefrom Cellulosimicrobium cellulans [Cellulosimicrobium cellulans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9ZG90 | 8.47e-40 | 789 | 1030 | 53 | 288 | Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1 |
P23903 | 3.91e-21 | 790 | 1031 | 421 | 681 | Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1 |
C1IE32 | 3.54e-18 | 792 | 1005 | 20 | 237 | Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1 |
P04957 | 1.99e-06 | 873 | 1031 | 100 | 242 | Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2 |
Q75A41 | 7.50e-06 | 860 | 980 | 185 | 295 | Probable glycosidase CRR1 OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=CRR1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000301 | 0.998999 | 0.000207 | 0.000167 | 0.000156 | 0.000147 |
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