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Conserved domains on  [gi|42573247|ref|NP_974720|]
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Carbohydrate-binding-like fold [Arabidopsis thaliana]

Protein Classification

CBM20 domain-containing protein( domain architecture ID 10144274)

CBM20 (family 20 carbohydrate-binding module) domain-containing protein may play a regulatory role in starch metabolism or glycogen metabolism

Gene Ontology:  GO:2001070
PubMed:  10452542|17013558|19682075|17084392

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 88-182 2.55e-29

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.


:

Pssm-ID: 119437  Cd Length: 96  Bit Score: 108.92  E-value: 2.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  88 RVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNWSD-GNVWT--VDLDLPVGRLVEFKLLLKAQTGEILWQPGPN 164
Cdd:cd05467   1 QVRFQVRCTTQFGQSVYVVGSHPELGN-WDPAKALRLNTSNsYPLWTgeIPLPAPEGQVIEYKYVIVDDDGNVQWESGSN 79

                        90
                ....*....|....*...
gi 42573247 165 RALETWETNKTIrICEDW 182
Cdd:cd05467  80 RVLTVPSTSSLI-VVDDW 96
 
Name Accession Description Interval E-value
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 88-182 2.55e-29

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.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 108.92  E-value: 2.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  88 RVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNWSD-GNVWT--VDLDLPVGRLVEFKLLLKAQTGEILWQPGPN 164
Cdd:cd05467   1 QVRFQVRCTTQFGQSVYVVGSHPELGN-WDPAKALRLNTSNsYPLWTgeIPLPAPEGQVIEYKYVIVDDDGNVQWESGSN 79

                        90
                ....*....|....*...
gi 42573247 165 RALETWETNKTIrICEDW 182
Cdd:cd05467  80 RVLTVPSTSSLI-VVDDW 96
CBM_2 smart01065
Starch binding domain;
87-171 3.43e-19

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 81.24  E-value: 3.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247     87 VRVRFQLRKECV-FGEHFFIVGDDPVFGGlWDPETALPLNWSDGN--VWTVDLDLP-VGRLVEFKLLLKAQTGEILWQPG 162
Cdd:smart01065   1 VSVTFKVRNGYTqPGESVYVVGSVPELGN-WNPKKAVPLSPDTDGypLWKGTVSLPpAGTTIEYKYVKVDEDGSVTWESG 79


                   ....*....
gi 42573247    163 PNRALETWE 171
Cdd:smart01065  80 PNRRLTVPE 88
CBM_20 pfam00686
Starch binding domain;
87-175 3.47e-19

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 81.56  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247    87 VRVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNW---SDGNVWTVDLDLPVGRLVEFKLLLKAQTGEILWQPGP 163
Cdd:pfam00686   1 VSVTFNVNATTQYGQSVYIVGSIPELGN-WNPKKAIALSAseySSYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESGP 79

                          90
                  ....*....|..
gi 42573247   164 NRALETWETNKT 175
Cdd:pfam00686  80 NRSYTVPASGAS 91
 
Name Accession Description Interval E-value
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 88-182 2.55e-29

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.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 108.92  E-value: 2.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  88 RVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNWSD-GNVWT--VDLDLPVGRLVEFKLLLKAQTGEILWQPGPN 164
Cdd:cd05467   1 QVRFQVRCTTQFGQSVYVVGSHPELGN-WDPAKALRLNTSNsYPLWTgeIPLPAPEGQVIEYKYVIVDDDGNVQWESGSN 79

                        90
                ....*....|....*...
gi 42573247 165 RALETWETNKTIrICEDW 182
Cdd:cd05467  80 RVLTVPSTSSLI-VVDDW 96
CBM_2 smart01065
Starch binding domain;
87-171 3.43e-19

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 81.24  E-value: 3.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247     87 VRVRFQLRKECV-FGEHFFIVGDDPVFGGlWDPETALPLNWSDGN--VWTVDLDLP-VGRLVEFKLLLKAQTGEILWQPG 162
Cdd:smart01065   1 VSVTFKVRNGYTqPGESVYVVGSVPELGN-WNPKKAVPLSPDTDGypLWKGTVSLPpAGTTIEYKYVKVDEDGSVTWESG 79


                   ....*....
gi 42573247    163 PNRALETWE 171
Cdd:smart01065  80 PNRRLTVPE 88
CBM_20 pfam00686
Starch binding domain;
87-175 3.47e-19

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 81.56  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247    87 VRVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNW---SDGNVWTVDLDLPVGRLVEFKLLLKAQTGEILWQPGP 163
Cdd:pfam00686   1 VSVTFNVNATTQYGQSVYIVGSIPELGN-WNPKKAIALSAseySSYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESGP 79

                          90
                  ....*....|..
gi 42573247   164 NRALETWETNKT 175
Cdd:pfam00686  80 NRSYTVPASGAS 91
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 82-175 8.83e-17

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.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 75.39  E-value: 8.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  82 ASNKTVRVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLN---WSDGN-VWTVDLDLPVGRLVEFKLLLKAQTGEI 157
Cdd:cd05811   2 ATATTVAVTFNERVTTSYGENIKIVGSIPQLGN-WDTSSAVALSasqYTSSNpLWSVTIPLPAGTSFEYKFIRKESDGSV 80

                        90
                ....*....|....*...
gi 42573247 158 LWQPGPNRALETWETNKT 175
Cdd:cd05811  81 TWESDPNRSYTVPSGCGT 98
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 87-169 5.43e-15

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.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 70.09  E-value: 5.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  87 VRVRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNWSDGNVWTVDLDLPVGRLVEFKLLLKAQTGEILWQPGPNRA 166
Cdd:cd05808   1 VAVTFNVTATTVWGQNVYVVGNVPELGN-WSPANAVALSAATYPVWSGTVDLPAGTAIEYKYIKKDGSGTVTWESGPNRT 79


                ...
gi 42573247 167 LET 169
Cdd:cd05808  80 ATT 82
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 89-179 2.92e-14

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. 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.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 68.27  E-value: 2.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  89 VRFQLRKECVFGEHFFIVGDDPVFGGlWDPETALPLNWSDGNVWTVDLDLPVGRLVEFKLLLKA--QTGEILWQPGPNRA 166
Cdd:cd05817   2 VTFKIHYPTQFGEAVYISGNCNQLGN-WNPSKAKRMQWNEGDLWTVDVGIPESVYIEYKYFVSNydDPNTVLWESGPNRV 80

                        90       100
                ....*....|....*....|
gi 42573247 167 LET-------WETNKTIRIC 179
Cdd:cd05817  81 LRTnhqilliWNHRKVKFNC 100
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 87-168 5.54e-13

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. 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.


Pssm-ID: 99892  Cd Length: 92  Bit Score: 64.06  E-value: 5.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  87 VRVRFQLRKECVFGEHFFIVGDDPVFGGlWdpETALPLNWSDgNVWTVDLDLPVGRLVEFKLLLKAQTGEILWQPGPNRA 166
Cdd:cd05818   2 VKLQVRLDHQVKFGEHVAILGSTKELGS-W--KKKVPMNWTE-NGWVCDLELDGGELVEYKFVIVKRDGSVIWEGGNNRV 77


                ..
gi 42573247 167 LE 168
Cdd:cd05818  78 LE 79
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
 85-184 5.78e-09

Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. 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.


Pssm-ID: 99893  Cd Length: 103  Bit Score: 53.37  E-value: 5.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  85 KTVRVRFQLRK--ECVFGEHFFIVGDDPVFGGlWDPET---ALPL---NWSDgnvWTVDLDLPVGRLVEFKLLLKAQTGE 156
Cdd:cd05820   1 KQIPVIFTVQNtpETAPGEFLYLTGSVPELGN-WSTSTdqaVGPLlcpNWPD---WFVVASVPAGTYIEFKFLKAPADGT 76

                        90       100
                ....*....|....*....|....*...
gi 42573247 157 ILWQPGPNRALETwETNKTIRICEDWDN 184
Cdd:cd05820  77 GTWEGGSNHAYTT-PSGGTGTVTVTWQR 103
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 87-182 1.53e-08

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. 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.


Pssm-ID: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 51.79  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  87 VRVRFQLRK-ECVFGEHFFIVGDDPVFGGlWDPETAL-----PLNWSDGNvWTVDLDLPVGRLVEFKLLLKAQTGEILWQ 160
Cdd:cd05807   3 VSVRFVVNNaTTQLGENVYLVGNVHELGN-WDPSKAIgpffnQVVYQYPN-WYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80

                        90       100
                ....*....|....*....|..
gi 42573247 161 PGPNRALETwETNKTIRICEDW 182
Cdd:cd05807  81 SGSNHTYTA-PSSTTGTIRVNW 101
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 104-182 2.25e-08

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. 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.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 51.56  E-value: 2.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247 104 FIVGDDPVFGGlWDPETALPLNWSDGNVWTVDLDLPVGRL-VEFK-LLLKAQTGEILWQPGPNRALETWETNKTIR--IC 179
Cdd:cd05816  18 YVTGSSPELGN-WDPQKALKLSDVGFPIWEADIDISKDSFpFEYKyIIANKDSGVVSWENGPNRELSAPSLKGESStlIV 96


                ...
gi 42573247 180 EDW 182
Cdd:cd05816  97 SDG 99
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 86-181 1.13e-06

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. 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.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 46.93  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  86 TVRVRF-QLRKecvfGEHFFIVGDDPVFGgLWDPETALPL--NWSDGNVWTVDLDLPVGRLVEFKLLLkaqtGEILWQPG 162
Cdd:cd05814   4 TFRVFAsELAP----GEVVAVVGSLPVLG-NWQPEKAVPLekEDDDCNLWKASIELPRGVDFQYRYFV----AVVLNDSG 74

                        90       100
                ....*....|....*....|...
gi 42573247 163 PNRAL-ETWETN---KTIRICED 181
Cdd:cd05814  75 PCQVIvRKWETHlqpRSIKPLEE 97
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 99-169 1.14e-06

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. 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.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 46.63  E-value: 1.14e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42573247  99 FGEHFFIVGDDPVFGGlWDPETALPLNWSDGNVWTVDLDLPVGRLVEFKLLLKAQTG---EILWQPGPNRALET 169
Cdd:cd05810  14 LGQSVYVVGNVPQLGN-WSPADAVKLDPTAYPTWSGSISLPASTNVEWKCLKRNETNptaGVQWQGGGNNQLTT 86
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
 87-150 2.30e-05

N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199892 [Multi-domain]  Cd Length: 86  Bit Score: 42.61  E-value: 2.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42573247  87 VRVRFQLRKEcVFGEHFFIVGDdpvFGGlWDPEtALPLNWSDGNVWTVDLDLPVGRLVEFKLLL 150
Cdd:cd07184   1 CKVTFELPAE-QGADSVSLVGD---FND-WDPQ-ATPMKKLKNGTFSATLDLPAGREYQFRYLI 58
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
 99-164 1.24e-04

Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 14, which hydrolyzes the alpha-1,4-glucosidic bonds of starch, yielding beta-maltose from the nonreducing end of the substrate. Beta-amylase is found in both plants and microorganisms, however the plant members lack a C-terminal CBM20 domain and are not included in this group. 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.


Pssm-ID: 99884  Cd Length: 99  Bit Score: 40.69  E-value: 1.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573247  99 FGEHFFIVGDDPVFGGlWDPETAlPL---NWSDGNVWTVDLDLPVGRLVEFKLLLKAQTGE-ILWQPGPN 164
Cdd:cd05809  16 IGETVYITGSRAELGN-WDTKQY-PIqlyYNSHSNDWRGTVHLPAGRNIEFKAIKKSKDGTnKSWQGGQQ 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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