Species | Ruminiclostridium_E sp900556525 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminiclostridium_E; Ruminiclostridium_E sp900556525 | |||||||||||
CAZyme ID | MGYG000002661_00602 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 11292; End: 12101 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 66 | 261 | 2.9e-89 | 0.9563106796116505 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd02175 | GH16_lichenase | 3.65e-120 | 66 | 265 | 10 | 212 | lichenase, member of glycosyl hydrolase family 16. Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure. |
pfam00722 | Glyco_hydro_16 | 2.79e-54 | 85 | 250 | 1 | 161 | Glycosyl hydrolases family 16. |
COG2273 | BglS | 7.56e-50 | 43 | 268 | 31 | 270 | Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]. |
cd00413 | Glyco_hydrolase_16 | 8.99e-47 | 63 | 257 | 1 | 201 | 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. |
cd02183 | GH16_fungal_CRH1_transglycosylase | 1.17e-27 | 85 | 238 | 12 | 166 | glycosylphosphatidylinositol-glucanosyltransferase. Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EGC02853.1 | 1.30e-112 | 66 | 267 | 65 | 264 |
ADU22000.1 | 7.91e-109 | 6 | 267 | 4 | 263 |
CCO06214.1 | 9.33e-106 | 1 | 265 | 1 | 253 |
ADD61790.1 | 5.75e-105 | 1 | 267 | 3 | 257 |
QEH67120.1 | 2.69e-103 | 1 | 268 | 1 | 256 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3WVJ_A | 3.71e-91 | 66 | 263 | 17 | 213 | ChainA, Beta-glucanase [Acetivibrio thermocellus ATCC 27405],3WVJ_B Chain B, Beta-glucanase [Acetivibrio thermocellus ATCC 27405] |
3I4I_A | 5.58e-89 | 66 | 263 | 33 | 231 | Crystalstructure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14],3I4I_B Crystal structure of a prokaryotic beta-1,3-1,4-glucanase (lichenase) derived from a mouse hindgut metagenome [uncultured murine large bowel bacterium BAC 14] |
3O5S_A | 3.42e-86 | 72 | 264 | 45 | 236 | CrystalStructure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis] |
1BYH_A | 4.38e-86 | 66 | 265 | 15 | 213 | MOLECULARAND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE [synthetic construct],1GLH_A Cation Binding To A Bacillus (1,3-1,4)-Beta-Glucanase. Geometry, Affinity And Effect On Protein Stability [Paenibacillus macerans],2AYH_A Crystal And Molecular Structure At 1.6 Angstroms Resolution Of The Hybrid Bacillus Endo-1,3-1,4-Beta-D-Glucan 4- Glucanohydrolase H(A16-M) [hybrid] |
1MAC_A | 5.81e-86 | 69 | 265 | 16 | 211 | CrystalStructure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans],1MAC_B Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A3DBX3 | 8.40e-89 | 66 | 263 | 46 | 242 | Beta-glucanase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=licB PE=1 SV=1 |
O14412 | 3.10e-88 | 66 | 265 | 47 | 242 | Beta-glucanase OS=Orpinomyces sp. (strain PC-2) OX=50059 GN=licA PE=1 SV=1 |
Q84C00 | 1.93e-87 | 66 | 263 | 46 | 242 | Beta-glucanase OS=Acetivibrio thermocellus OX=1515 GN=licB PE=1 SV=1 |
Q53317 | 7.53e-86 | 69 | 263 | 586 | 786 | Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2 |
P04957 | 2.14e-85 | 72 | 264 | 49 | 240 | Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000000 | 1.000043 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.