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Conserved domains on  [gi|41688530|sp|O95210|]
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RecName: Full=Starch-binding domain-containing protein 1; AltName: Full=Genethonin-1; AltName: Full=Glycophagy cargo receptor STBD1

Protein Classification

starch-binding domain-containing protein 1( domain architecture ID 10146617)

starch-binding domain-containing protein 1 (STBD1) acts as a cargo receptor for glycogen and delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes

Gene Symbol:  STBD1
Gene Ontology:  GO:2001070
PubMed:  19682075|20810658

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 264-358 1.37e-62

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 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: 99887  Cd Length: 95  Bit Score: 194.64  E-value: 1.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLE 343
Cdd:cd05813   1 VNVTFRVHYITHSDAQLVAVTGDHEELGSWHSYIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQVTRWEECSNRLLE 80

                        90
                ....*....|....*
gi 41688530 344 TGHEDKVVHAWWGIH 358
Cdd:cd05813  81 TGHEDKIVHKWWGCH 95
 
Name Accession Description Interval E-value
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 264-358 1.37e-62

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 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: 99887  Cd Length: 95  Bit Score: 194.64  E-value: 1.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLE 343
Cdd:cd05813   1 VNVTFRVHYITHSDAQLVAVTGDHEELGSWHSYIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQVTRWEECSNRLLE 80

                        90
                ....*....|....*
gi 41688530 344 TGHEDKVVHAWWGIH 358
Cdd:cd05813  81 TGHEDKIVHKWWGCH 95
CBM_2 smart01065
Starch binding domain;
264-346 2.25e-25

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 97.80  E-value: 2.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530    264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNT--YIPLHYNKDGF--WSHSI-FLPADTVVEWKFVLVENGGVTRWEECS 338
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPkkAVPLSPDTDGYplWKGTVsLPPAGTTIEYKYVKVDEDGSVTWESGP 80


                   ....*...
gi 41688530    339 NRFLETGH 346
Cdd:smart01065  81 NRRLTVPE 88
CBM_20 pfam00686
Starch binding domain;
264-354 2.60e-24

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 95.05  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530   264 VSVRFQVHYVTsTDVQFIAVTGDHECLGRWNT--YIPLHYNKDG---FWSHSIFLPADTVVEWKFVLVENGGVTRWEECS 338
Cdd:pfam00686   1 VSVTFNVNATT-QYGQSVYIVGSIPELGNWNPkkAIALSASEYSsypLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESGP 79

                          90
                  ....*....|....*.
gi 41688530   339 NRFLETGHEDKVVHAW 354
Cdd:pfam00686  80 NRSYTVPASGASTTTT 95
 
Name Accession Description Interval E-value
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 264-358 1.37e-62

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 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: 99887  Cd Length: 95  Bit Score: 194.64  E-value: 1.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLE 343
Cdd:cd05813   1 VNVTFRVHYITHSDAQLVAVTGDHEELGSWHSYIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQVTRWEECSNRLLE 80

                        90
                ....*....|....*
gi 41688530 344 TGHEDKVVHAWWGIH 358
Cdd:cd05813  81 TGHEDKIVHKWWGCH 95
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 265-355 1.74e-25

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: 98.52  E-value: 1.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 265 SVRFQVHYvTSTDVQFIAVTGDHECLGRWNTY--IPLHYNKDG-FWSHSIFLPA--DTVVEWKFVLVENGGVTRWEECSN 339
Cdd:cd05467   1 QVRFQVRC-TTQFGQSVYVVGSHPELGNWDPAkaLRLNTSNSYpLWTGEIPLPApeGQVIEYKYVIVDDDGNVQWESGSN 79

                        90
                ....*....|....*..
gi 41688530 340 RFLETGHEDK-VVHAWW 355
Cdd:cd05467  80 RVLTVPSTSSlIVVDDW 96
CBM_2 smart01065
Starch binding domain;
264-346 2.25e-25

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 97.80  E-value: 2.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530    264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNT--YIPLHYNKDGF--WSHSI-FLPADTVVEWKFVLVENGGVTRWEECS 338
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPkkAVPLSPDTDGYplWKGTVsLPPAGTTIEYKYVKVDEDGSVTWESGP 80


                   ....*...
gi 41688530    339 NRFLETGH 346
Cdd:smart01065  81 NRRLTVPE 88
CBM_20 pfam00686
Starch binding domain;
264-354 2.60e-24

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 95.05  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530   264 VSVRFQVHYVTsTDVQFIAVTGDHECLGRWNT--YIPLHYNKDG---FWSHSIFLPADTVVEWKFVLVENGGVTRWEECS 338
Cdd:pfam00686   1 VSVTFNVNATT-QYGQSVYIVGSIPELGNWNPkkAIALSASEYSsypLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESGP 79

                          90
                  ....*....|....*.
gi 41688530   339 NRFLETGHEDKVVHAW 354
Cdd:pfam00686  80 NRSYTVPASGASTTTT 95
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 264-345 2.86e-10

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: 56.60  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVhYVTSTDVQFIAVTGDHECLGRWNT--YIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRF 341
Cdd:cd05808   1 VAVTFNV-TATTVWGQNVYVVGNVPELGNWSPanAVALSAATYPVWSGTVDLPAGTAIEYKYIKKDGSGTVTWESGPNRT 79


                ....
gi 41688530 342 LETG 345
Cdd:cd05808  80 ATTP 83
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 279-342 9.25e-10

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: 55.02  E-value: 9.25e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688530 279 QFIAVTGDHECLGRWNT--YIPLHYNKDGFWSHSIFLPADTV-VEWKFVLVENG-GVTRWEECSNRFL 342
Cdd:cd05816  15 QSVYVTGSSPELGNWDPqkALKLSDVGFPIWEADIDISKDSFpFEYKYIIANKDsGVVSWENGPNREL 82
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 264-355 4.12e-08

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: 50.73  E-value: 4.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVHyVTSTDVQFIAVTGDHECLGRWNTY--IPLHYNK----DGFWSHSIFLPADTVVEWKFVLVENGGVTRWEEC 337
Cdd:cd05811   7 VAVTFNER-VTTSYGENIKIVGSIPQLGNWDTSsaVALSASQytssNPLWSVTIPLPAGTSFEYKFIRKESDGSVTWESD 85

                        90       100
                ....*....|....*....|.
gi 41688530 338 SNRFLETGHE---DKVVHAWW 355
Cdd:cd05811  86 PNRSYTVPSGcgtTATVDDSW 106
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 269-343 9.83e-07

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: 46.34  E-value: 9.83e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688530 269 QVHYVTSTDVQF---IAVTGDHECLGRWNTYIPLHYNKDGfWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLE 343
Cdd:cd05818   3 KLQVRLDHQVKFgehVAILGSTKELGSWKKKVPMNWTENG-WVCDLELDGGELVEYKFVIVKRDGSVIWEGGNNRVLE 79
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 266-357 1.68e-06

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: 45.93  E-value: 1.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 266 VRFQVHYVTstdvQF---IAVTGDHECLGRWNTY--IPLHYNKDGFWSHSIFLPADTVVEWKFVL--VENGGVTRWEECS 338
Cdd:cd05817   2 VTFKIHYPT----QFgeaVYISGNCNQLGNWNPSkaKRMQWNEGDLWTVDVGIPESVYIEYKYFVsnYDDPNTVLWESGP 77

                        90
                ....*....|....*....
gi 41688530 339 NRFLETGHEDKVVHAWWGI 357
Cdd:cd05817  78 NRVLRTNHQILLIWNHRKV 96
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 263-345 6.39e-06

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: 44.47  E-value: 6.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 263 QVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNT--YIPLHYNKDGF----WSHSIFLPADTVVEWKFVLVENGGVTRWEE 336
Cdd:cd05807   2 QVSVRFVVNNATTQLGENVYLVGNVHELGNWDPskAIGPFFNQVVYqypnWYYDVSVPAGTTIEFKFIKKNGDNTVTWES 81


                ....*....
gi 41688530 337 CSNRFLETG 345
Cdd:cd05807  82 GSNHTYTAP 90
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
 262-339 4.97e-05

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: 41.82  E-value: 4.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 262 QQVSVRFQVHYVTSTDV-QFIAVTGDHECLGRW-----NTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWE 335
Cdd:cd05820   1 KQIPVIFTVQNTPETAPgEFLYLTGSVPELGNWststdQAVGPLLCPNWPDWFVVASVPAGTYIEFKFLKAPADGTGTWE 80


                ....
gi 41688530 336 ECSN 339
Cdd:cd05820  81 GGSN 84
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
 264-341 1.48e-03

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: 37.61  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 264 VSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYI-PL---HYNKDGFWSHSIFLPADTVVEWK-FVLVENGGVTRWEECS 338
Cdd:cd05809   3 VPQTFVVKNVPTTIGETVYITGSRAELGNWDTKQyPIqlyYNSHSNDWRGTVHLPAGRNIEFKaIKKSKDGTNKSWQGGQ 82


                ...
gi 41688530 339 NRF 341
Cdd:cd05809  83 QSW 85
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 266-335 8.13e-03

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: 35.76  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688530 266 VRFQVHYVTSTDVQFIAVTGDHECLGRWN--TYIPLHYNKDGF--WSHSIFLPADTVVEWKFVLVENGG--------VTR 333
Cdd:cd05814   3 VTFRVFASELAPGEVVAVVGSLPVLGNWQpeKAVPLEKEDDDCnlWKASIELPRGVDFQYRYFVAVVLNdsgpcqviVRK 82


                ..
gi 41688530 334 WE 335
Cdd:cd05814  83 WE 84
 
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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