Species | CAG-279 sp900550025 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-279; CAG-279 sp900550025 | |||||||||||
CAZyme ID | MGYG000004090_01756 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 63612; End: 64910 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 173 | 431 | 1.2e-68 | 0.991304347826087 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08023 | GH16_laminarinase_like | 4.67e-74 | 172 | 431 | 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. |
cd08024 | GH16_CCF | 1.52e-37 | 170 | 403 | 1 | 273 | 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 | 5.01e-21 | 166 | 403 | 1 | 229 | 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 | 1.08e-20 | 168 | 401 | 15 | 234 | Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]. |
pfam00722 | Glyco_hydro_16 | 5.32e-19 | 259 | 374 | 21 | 123 | Glycosyl hydrolases family 16. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AHF12786.1 | 2.24e-106 | 3 | 432 | 4 | 406 |
AHF12161.1 | 2.79e-105 | 7 | 432 | 5 | 420 |
AHF12785.1 | 1.05e-73 | 167 | 432 | 29 | 269 |
AHF12162.1 | 5.07e-70 | 170 | 432 | 1 | 254 |
QEC53190.1 | 5.05e-63 | 167 | 432 | 36 | 275 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ILN_A | 1.51e-50 | 169 | 432 | 6 | 248 | ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus] |
6XOF_A | 7.02e-44 | 163 | 432 | 20 | 267 | ChainA, GH16 family protein [uncultured bacterium] |
6XQF_A | 3.76e-43 | 163 | 432 | 20 | 267 | ChainA, GH16 family protein [uncultured bacterium],6XQG_A Chain A, GH16 family protein [uncultured bacterium],6XQH_A Chain A, GH16 family protein [uncultured bacterium],6XQL_A Chain A, GH16 family protein [uncultured bacterium],6XQM_A Chain A, GH16 family protein [uncultured bacterium] |
4DFS_A | 7.54e-41 | 169 | 432 | 19 | 263 | Structureof the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4DFS_B Structure of the catalytic domain of an endo-1,3-beta-glucanase (laminarinase) from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1] |
3AZX_A | 1.20e-40 | 169 | 432 | 11 | 255 | Crystalstructure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZX_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZY_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3AZZ_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3AZZ_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with gluconolactone [Thermotoga maritima MSB8],3B00_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B00_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 in complex with cetyltrimethylammonium bromide [Thermotoga maritima MSB8],3B01_A Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_B Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_C Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8],3B01_D Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 [Thermotoga maritima MSB8] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P45798 | 9.85e-52 | 169 | 432 | 41 | 283 | Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1 |
P23903 | 1.06e-47 | 170 | 432 | 425 | 680 | Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1 |
Q9ZG90 | 1.21e-30 | 169 | 432 | 57 | 288 | Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1 |
C1IE32 | 1.72e-28 | 150 | 429 | 2 | 265 | Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1 |
Q8N0N3 | 1.09e-18 | 258 | 427 | 131 | 327 | Beta-1,3-glucan-binding protein OS=Penaeus monodon OX=6687 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000478 | 0.998540 | 0.000260 | 0.000246 | 0.000227 | 0.000208 |
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