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CAZyme Information: QRD05980.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Parastagonospora nodorum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum | |||||||||||
| CAZyme ID | QRD05980.1 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | CBM20 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2IA00] | |||||||||||
| CAZyme Property |
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| Genome Property |
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Enzyme Prediction help
| EC | 3.2.1.1:13 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM20 | 127 | 217 | 1.9e-27 | 0.9666666666666667 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 99886 | CBM20_glucoamylase | 7.19e-47 | 124 | 225 | 4 | 106 | 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 | 7.08e-36 | 127 | 222 | 1 | 95 | Starch binding domain. |
| 119437 | CBM20 | 7.15e-27 | 128 | 225 | 1 | 96 | 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. |
| 215006 | CBM_2 | 2.25e-26 | 127 | 214 | 1 | 88 | Starch binding domain. |
| 99883 | CBM20_alpha_amylase | 5.64e-25 | 127 | 225 | 1 | 94 | Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.16e-91 | 1 | 226 | 362 | 587 | |
| 1.79e-89 | 1 | 226 | 356 | 582 | |
| 3.20e-81 | 1 | 218 | 362 | 579 | |
| 1.75e-67 | 1 | 226 | 361 | 600 | |
| 1.25e-57 | 1 | 226 | 359 | 586 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7.77e-24 | 124 | 226 | 4 | 108 | GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, MINIMIZED AVERAGE STRUCTURE [Aspergillus niger],1ACZ_A GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, 5 STRUCTURES [Aspergillus niger],1KUL_A Chain A, GLUCOAMYLASE [Aspergillus niger],1KUM_A Chain A, GLUCOAMYLASE [Aspergillus niger],5GHL_A Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_B Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_C Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger],5GHL_D Crystal structure Analysis of the starch-binding domain of glucoamylase from Aspergillus niger [Aspergillus niger] |
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| 1.70e-23 | 124 | 226 | 494 | 598 | Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei] |
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| 1.06e-18 | 130 | 226 | 518 | 616 | Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger] |
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| 2.15e-18 | 1 | 91 | 361 | 449 | Chain A, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa] |
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| 2.47e-11 | 120 | 219 | 502 | 599 | Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.46e-25 | 124 | 226 | 509 | 612 | Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2 |
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| 2.26e-22 | 127 | 226 | 526 | 626 | Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3 |
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| 1.06e-21 | 124 | 226 | 535 | 639 | Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1 |
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| 2.66e-21 | 124 | 226 | 535 | 639 | Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1 |
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| 5.51e-18 | 130 | 226 | 542 | 640 | Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000046 | 0.000001 |