Species | Cladophialophora bantiana | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora bantiana | |||||||||||
CAZyme ID | KIW91308.1 | |||||||||||
CAZy Family | GH154 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.3:94 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH15 | 57 | 455 | 8.4e-73 | 0.9473684210526315 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
395586 | Glyco_hydro_15 | 4.05e-115 | 37 | 457 | 1 | 417 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
99886 | CBM20_glucoamylase | 7.41e-18 | 513 | 609 | 9 | 104 | Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
395557 | CBM_20 | 2.28e-13 | 513 | 604 | 3 | 91 | Starch binding domain. |
119437 | CBM20 | 4.34e-11 | 513 | 606 | 2 | 92 | The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. |
225922 | SGA1 | 1.74e-10 | 60 | 453 | 261 | 598 | Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.92e-189 | 10 | 606 | 13 | 600 | |
1.92e-189 | 10 | 606 | 13 | 600 | |
1.92e-189 | 10 | 606 | 13 | 600 | |
7.72e-189 | 28 | 609 | 32 | 604 | |
7.83e-186 | 28 | 612 | 32 | 604 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.64e-191 | 10 | 606 | 13 | 600 | Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae] |
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1.52e-156 | 28 | 615 | 8 | 594 | Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2] |
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9.75e-155 | 26 | 603 | 1 | 606 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
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2.89e-152 | 31 | 601 | 5 | 587 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
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2.94e-146 | 26 | 505 | 1 | 469 | Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.41e-190 | 10 | 606 | 13 | 600 | Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1 |
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6.46e-155 | 24 | 602 | 23 | 628 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
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3.76e-154 | 24 | 603 | 23 | 630 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
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3.76e-154 | 24 | 603 | 23 | 630 | Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1 |
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2.90e-153 | 24 | 602 | 23 | 628 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000517 | 0.999467 | CS pos: 24-25. Pr: 0.9689 |
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