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Conserved domains on  [gi|298676470|ref|NP_001177333|]
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amylase 2b isoform 2 precursor [Mus musculus]

Protein Classification

alpha-amylase( domain architecture ID 10183021)

alpha-amylase catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides

CATH:  3.20.20.80|2.60.40.1180
CAZY:  GH13
EC:  3.2.1.1
Gene Ontology:  GO:0004556|GO:0005975
PubMed:  21544166|17085431|11257505
SCOP:  4003138|4002636

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-336 3.26e-149

Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


:

Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 426.59  E-value: 3.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENIVIhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 105 GVRIYVDAVINHMCGSGNP------AG-----TSS-----TCGSYLN-------------------PNnrefpavpysaw 149
Cdd:cd11317   79 GVRVYVDAVINHMAGDANEvrncelVGladlnTESdyvrdKIADYLNdlislgvagfridaakhmwPE------------ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 150 DFND-----NKCNGEISNYN-DAYQ-VIDLGGEAIKGSEYFGNGRVTEFKFGAKLGTVIRKWNGEKmsYLKNWGEGWGLV 222
Cdd:cd11317  147 DLAAilarlKDLNGGPLGSRpYIYQeVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 223 PSDRALVFVDNHDNQRGHGAGGSsILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGV 301
Cdd:cd11317  225 PSERAVVFVDNHDNQRGHGGGGD-MLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFS---------DSDQGPPSDgSGN 294

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 298676470 302 TKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 336
Cdd:cd11317  295 TLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
342-430 8.07e-31

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 8.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470   342 ANWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLKVNVGSDGKAHFSISNSAEdp 421
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 298676470   422 fIAIHADSK 430
Cdd:smart00632  74 -VAIHVDAK 81
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-336 3.26e-149

Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 426.59  E-value: 3.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENIVIhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 105 GVRIYVDAVINHMCGSGNP------AG-----TSS-----TCGSYLN-------------------PNnrefpavpysaw 149
Cdd:cd11317   79 GVRVYVDAVINHMAGDANEvrncelVGladlnTESdyvrdKIADYLNdlislgvagfridaakhmwPE------------ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 150 DFND-----NKCNGEISNYN-DAYQ-VIDLGGEAIKGSEYFGNGRVTEFKFGAKLGTVIRKWNGEKmsYLKNWGEGWGLV 222
Cdd:cd11317  147 DLAAilarlKDLNGGPLGSRpYIYQeVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 223 PSDRALVFVDNHDNQRGHGAGGSsILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGV 301
Cdd:cd11317  225 PSERAVVFVDNHDNQRGHGGGGD-MLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFS---------DSDQGPPSDgSGN 294

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 298676470 302 TKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 336
Cdd:cd11317  295 TLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
342-430 8.07e-31

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 8.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470   342 ANWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLKVNVGSDGKAHFSISNSAEdp 421
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 298676470   422 fIAIHADSK 430
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-121 1.57e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 110.11  E-value: 1.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470    28 IVHLFEWR-------WVDIAKECErYLAPKGFGGVQVSPPNENIvihnPSRPWWERYQPISYK-ICTRSGNEDEFRDMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 298676470   100 RCNNVGVRIYVDAVINHMCGSG 121
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 341-428 3.56e-17

Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 76.22  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  341 FANWWDNNSNQVAFSRGN---RGFIVFNNDDWALSATLQTGLP-AGTYCDVISGDKV--DGNCTGLKVNVGSDGKAHFSI 414
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 298676470  415 SNSAEDPFIAIHAD 428
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
PRK14705 PRK14705
glycogen branching enzyme; Provisional
 15-116 2.06e-06

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 50.38  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470   15 AQYDPHTSDGRTAIVHLFEWR----WVDIAKECERYLAPKGFGGVQVSPpneniVIHNPSRPWWErYQPISYKICT-RSG 89
Cdd:PRK14705  739 AERDPHNSPMSVYEVHLGSWRlglgYRELAKELVDYVKWLGFTHVEFMP-----VAEHPFGGSWG-YQVTSYFAPTsRFG 812

                          90       100
                  ....*....|....*....|....*..
gi 298676470   90 NEDEFRDMVTRCNNVGVRIYVDAVINH 116
Cdd:PRK14705  813 HPDEFRFLVDSLHQAGIGVLLDWVPAH 839
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-336 3.26e-149

Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 426.59  E-value: 3.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  25 RTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENIVIhnPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVG--PGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 105 GVRIYVDAVINHMCGSGNP------AG-----TSS-----TCGSYLN-------------------PNnrefpavpysaw 149
Cdd:cd11317   79 GVRVYVDAVINHMAGDANEvrncelVGladlnTESdyvrdKIADYLNdlislgvagfridaakhmwPE------------ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 150 DFND-----NKCNGEISNYN-DAYQ-VIDLGGEAIKGSEYFGNGRVTEFKFGAKLGTVIRKWNGEKmsYLKNWGEGWGLV 222
Cdd:cd11317  147 DLAAilarlKDLNGGPLGSRpYIYQeVIDGGGEAIQPSEYTGNGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 223 PSDRALVFVDNHDNQRGHGAGGSsILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNrnfqngkdqNDWIGPPNN-NGV 301
Cdd:cd11317  225 PSERAVVFVDNHDNQRGHGGGGD-MLTYKDGRRYKLANAFMLAWPYGTPRVMSSYYFS---------DSDQGPPSDgSGN 294

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 298676470 302 TKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVV 336
Cdd:cd11317  295 TLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
342-430 8.07e-31

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.49  E-value: 8.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470   342 ANWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISgdkvdGNCTGLKVNVGSDGKAHFSISNSAEdp 421
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 298676470   422 fIAIHADSK 430
Cdd:smart00632  74 -VAIHVDAK 81
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 27-340 8.70e-29

Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200454 [Multi-domain]  Cd Length: 352  Bit Score: 115.84  E-value: 8.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  27 AIVHLFEWRWVDIAKECERyLAPKGFGGVQVSPPNENIVIHNPSRPWWERYQPISYKICTRS-GNEDEFRDMVTRCNNVG 105
Cdd:cd11315    3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 106 VRIYVDAVINHMCGSGNpagtsstcgsylNPNNREFPAVPYSAWDFNDNKCNGEISNYNDAYQV---------------- 169
Cdd:cd11315   82 IKIIVDVVFNHMANEGS------------AIEDLWYPSADIELFSPEDFHGNGGISNWNDRWQVtqgrlgglpdlntenp 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 170 -------------IDLG----------------------------------------GEAIKG--------SEYFGNGRV 188
Cdd:cd11315  150 avqqqqkaylkalVALGvdgfrfdaakhielpdepskasdfwtnilnnldkdglfiyGEVLQDggsrdsdyASYLSLGGV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 189 TEFKFGAKL-GTVIRKWNGEKMSYLKNWGEGwglVPSDRALVFVDNHDNQrghgAGGSSILTFWDARMYKMAVGFMLAHP 267
Cdd:cd11315  230 TASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY----NNDGFESTGLDDEDERLAWAYLAARD 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298676470 268 YGFTRVmssyrWNRNfQNGKDQNDWIGPpnnngvtkevtinadttCGNDWVCEHrwrQIRNMVAFRNVVNGQP 340
Cdd:cd11315  303 GGTPLF-----FSRP-NGSGGTNPQIGD-----------------RGDDAWKSP---DVVAVNKFHNAMHGQP 349
Aamy smart00642
Alpha-amylase domain;
28-121 1.57e-28

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 110.11  E-value: 1.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470    28 IVHLFEWR-------WVDIAKECErYLAPKGFGGVQVSPPNENIvihnPSRPWWERYQPISYK-ICTRSGNEDEFRDMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 298676470   100 RCNNVGVRIYVDAVINHMCGSG 121
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDGG 99
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 341-428 3.56e-17

Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 76.22  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  341 FANWWDNNSNQVAFSRGN---RGFIVFNNDDWALSATLQTGLP-AGTYCDVISGDKV--DGNCTGLKVNVGSDGKAHFSI 414
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 298676470  415 SNSAEDPFIAIHAD 428
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-267 4.40e-10

Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 59.88  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  45 RYLAPKGFGGVQVSPPNENIVIHNPSRPWWERYqpiSYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHmcgsgnpa 124
Cdd:cd00551   32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 125 gtssTCGSYL-------------NPNNREFPAVPYSAWdfndNKCNGEIsnYNDAYQVidlgGEAIKGSEYFGNGRVTEF 191
Cdd:cd00551  101 ----DILRFWldegvdgfrldaaKHVPKPEPVEFLREI----RKDAKLA--KPDTLLL----GEAWGGPDELLAKAGFDD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470 192 KFGAKL-----GTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGSSILTFWDARMyKMAVGFMLAH 266
Cdd:cd00551  167 GLDSVFdfpllEALRDALKGGEGALAILAALLLLNPEGALLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTL 245


                 .
gi 298676470 267 P 267
Cdd:cd00551  246 P 246
PRK14705 PRK14705
glycogen branching enzyme; Provisional
 15-116 2.06e-06

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 50.38  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470   15 AQYDPHTSDGRTAIVHLFEWR----WVDIAKECERYLAPKGFGGVQVSPpneniVIHNPSRPWWErYQPISYKICT-RSG 89
Cdd:PRK14705  739 AERDPHNSPMSVYEVHLGSWRlglgYRELAKELVDYVKWLGFTHVEFMP-----VAEHPFGGSWG-YQVTSYFAPTsRFG 812

                          90       100
                  ....*....|....*....|....*..
gi 298676470   90 NEDEFRDMVTRCNNVGVRIYVDAVINH 116
Cdd:PRK14705  813 HPDEFRFLVDSLHQAGIGVLLDWVPAH 839
PLN02784 PLN02784
alpha-amylase
 21-139 8.72e-06

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 48.08  E-value: 8.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  21 TSDGRTAIVHLFEW------RWVDIAKECERYLAPKGFGGVQVSPPNENIvihNPsrpwwERYQPIS-YKICTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 298676470  94 FRDMVTRCNNVGVRIYVDAVINHMCGS-GNPAGTSSTCGSYLNPNNR 139
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHfQNQNGVWNIFGGRLNWDDR 616
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 82-120 1.88e-04

Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 42.98  E-value: 1.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 298676470  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGS 120
Cdd:cd11314   57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGP 95
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
 82-174 3.82e-04

Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200490 [Multi-domain]  Cd Length: 366  Bit Score: 42.55  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  82 YKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMcgsgnpagtsstcgsylnpnNREFPAvpysawdFNDNKCNGEIS 161
Cdd:cd11353   66 YKIDRRLGTNEDFKAVCKKLHENGIKVVLDGVFNHV--------------------GRDFFA-------FKDVQENRENS 118

                         90
                 ....*....|...
gi 298676470 162 NYNDAYQVIDLGG 174
Cdd:cd11353  119 PYKDWFKGVNFDG 131
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 51-171 3.90e-03

Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 39.09  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676470  51 GFGGVQVSPPNENIvihNPSRPWWERY-----QPIsYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGSGNPAG 125
Cdd:cd11319   56 GFDAIWISPIVKNI---EGNTAYGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSD 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 298676470 126 TSStcgSYLNPnnrefpavpysawdFNDNK-----CngEISNYNDAYQVID 171
Cdd:cd11319  132 VDY---SSFVP--------------FNDSSyyhpyC--WITDYNNQTSVED 163
 
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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