Species | Coccidioides immitis | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis | |||||||||||
CAZyme ID | TPX22802.1 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | GH16 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A6C1M6R0] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 124 | 283 | 1e-33 | 0.8541666666666666 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
185683 | Glyco_hydrolase_16 | 6.11e-39 | 67 | 283 | 5 | 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. |
185684 | GH16_lichenase | 1.16e-08 | 143 | 280 | 70 | 208 | 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. |
185693 | GH16_laminarinase_like | 4.88e-05 | 98 | 283 | 38 | 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. |
185687 | GH16_beta_agarase | 2.24e-04 | 78 | 240 | 37 | 204 | 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 |
---|---|---|---|---|---|
1.16e-80 | 141 | 343 | 1 | 188 | |
5.26e-29 | 21 | 301 | 9 | 301 | |
8.71e-29 | 23 | 313 | 5 | 277 | |
1.25e-28 | 23 | 287 | 10 | 292 | |
2.35e-28 | 23 | 313 | 5 | 277 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.11e-09 | 145 | 280 | 76 | 209 | Bacillus Licheniformis Beta-Glucanase [Bacillus licheniformis] |
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1.01e-08 | 145 | 280 | 100 | 233 | Crystal Structure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) [Bacillus subtilis] |
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4.68e-08 | 138 | 287 | 11 | 158 | NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans] |
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7.95e-08 | 138 | 279 | 11 | 153 | NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans] |
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8.34e-08 | 138 | 279 | 67 | 209 | Crystal Structure 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 |
---|---|---|---|---|---|---|
4.05e-08 | 145 | 283 | 105 | 240 | Beta-glucanase OS=Bacillus licheniformis OX=1402 GN=bg1 PE=1 SV=1 |
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5.41e-08 | 145 | 280 | 104 | 237 | Beta-glucanase OS=Bacillus subtilis (strain 168) OX=224308 GN=bglS PE=1 SV=2 |
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4.22e-07 | 145 | 272 | 101 | 225 | Beta-glucanase OS=Bacillus amyloliquefaciens OX=1390 GN=bglA PE=3 SV=1 |
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5.58e-07 | 138 | 279 | 92 | 234 | Beta-glucanase OS=Paenibacillus macerans OX=44252 PE=1 SV=2 |
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2.48e-06 | 145 | 279 | 100 | 235 | Beta-glucanase OS=Paenibacillus polymyxa OX=1406 GN=gluB PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.002428 | 0.997516 | CS pos: 33-34. Pr: 0.9569 |
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