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Conserved domains on  [gi|160358819|ref|NP_031472|]
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alpha-amylase 1 precursor [Mus musculus]

Protein Classification

alpha-amylase family protein( domain architecture ID 10183021)

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

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, ...
 25-416 0e+00

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: 582.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  25 RTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVvhSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 105 GVRIYVDAVINHMCGvgaqagqsstcgsyfnpnnrdfpgvpysgfdfndgkcrtasggienyqDAAQVRDCRLSGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 185 LEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAVSSNEYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 265 NGRVTEFKYGAKLGKVMRKWDGEKmsYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160358819 345 AHPYGFTRVMSSYYWPrnfqngkdvNDWVGPPNN-NGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVV 416
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.12e-32

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.49  E-value: 2.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   422 ANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISgdkvdGNCTGIKVYVGNDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 160358819   502 fIAIHAESK 510
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, ...
 25-416 0e+00

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: 582.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  25 RTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVvhSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 105 GVRIYVDAVINHMCGvgaqagqsstcgsyfnpnnrdfpgvpysgfdfndgkcrtasggienyqDAAQVRDCRLSGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 185 LEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAVSSNEYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 265 NGRVTEFKYGAKLGKVMRKWDGEKmsYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160358819 345 AHPYGFTRVMSSYYWPrnfqngkdvNDWVGPPNN-NGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVV 416
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.12e-32

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.49  E-value: 2.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   422 ANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISgdkvdGNCTGIKVYVGNDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 160358819   502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-121 2.95e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 107.42  E-value: 2.95e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819    28 IVHLFEWR-------WVDIAKECErYLAPNGFAGVQVSPPNENIVVhspsRPWWERYQPISYK-ICSRSGNEDEFRDMVN 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 160358819   100 RCNNVGVRIYVDAVINHMCGVG 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 ...
 421-508 2.90e-18

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: 79.69  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  421 FANWWDNDSNQVAFGRGN---KGFIVFNNDDWALSETLQTGLP-AGTYCDVISGDKV--DGNCTGIKVYVGNDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 160358819  495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
82-347 6.87e-17

Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 82.60  E-value: 6.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHmCGVG------AQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGK 155
Cdd:COG0366   69 RDVDPRFGTLADFDELVAEAHARGIKVILDLVLNH-TSDEhpwfqeARAGPDSPYRDWYVWRDGKPDLPPNNWFSIFGGS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 156 CRTASGGIENYqdaaqVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKLH 230
Cdd:COG0366  148 AWTWDPEDGQY-----YLHLFFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLR 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 231 NLNTKWFSQGSRPFIFQEVIDLGGEAVSsnEYFGNGR---VTEFKYGAKLGKVMRKWDGEKM-SYLKNWGEgwgLMPSDR 306
Cdd:COG0366  223 ELRAAVDEYYPDFFLVGEAWVDPPEDVA--RYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPA---LYPEGG 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 160358819 307 ALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366  298 WWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 2.78e-12

Alpha amylase, catalytic 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: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.77  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMcgvgaqagqsSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASG 161
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQESRSSKDNPYRDYYFWRPGGGPIPPN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  162 GIENYQDAAQVRDCRLSG----------LLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDK--- 228
Cdd:pfam00128 112 NWRSYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpf 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  229 ----LHNLNTKWFSQGSRpFIFQEV-IDLGGEAV--SSNEYFGNGRVTEFKYGAKLGKVMRKWDGEK--MSYLKNWGEGW 299
Cdd:pfam00128 192 whefTQAMNETVFGYKDV-MTVGEVfHGDGEWARvyTTEARMELEMGFNFPHNDVALKPFIKWDLAPisARKLKEMITDW 270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 160358819  300 --GLMPSDRALV-FVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 271 ldALPDTNGWNFtFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
PLN02784 PLN02784
alpha-amylase
 21-227 2.18e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.94  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  21 TQYGRTAIVHLFEW------RWVDIAKECERYLAPNGFAGVQVSPPNENIvvhSPsrpwwERYQPIS-YKICSRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  94 FRDMVNRCNNVGVRIYVDAVINHMCG-VGAQAGQSSTCGSYFNPNNR----DFPgvpysgfDFNdGKCRTASGgiENYQD 168
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAhFQNQNGVWNIFGGRLNWDDRavvaDDP-------HFQ-GRGNKSSG--DNFHA 639

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 169 AAQVRDcrlsglldlalEKDYVRTKVADYMNHLID-IGVAGFRLDASKHMWPGDIKAILD 227
Cdd:PLN02784 640 APNIDH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYME 688
 
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, ...
 25-416 0e+00

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: 582.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  25 RTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVvhSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNV 104
Cdd:cd11317    1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 105 GVRIYVDAVINHMCGvgaqagqsstcgsyfnpnnrdfpgvpysgfdfndgkcrtasggienyqDAAQVRDCRLSGLLDLA 184
Cdd:cd11317   79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 185 LEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFsqGSRPFIFQEVIDLGGEAVSSNEYFG 264
Cdd:cd11317  111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGGPL--GSRPYIYQEVIDGGGEAIQPSEYTG 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 265 NGRVTEFKYGAKLGKVMRKWDGEKmsYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317  189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160358819 345 AHPYGFTRVMSSYYWPrnfqngkdvNDWVGPPNN-NGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVV 416
Cdd:cd11317  266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 27-420 1.94e-49

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: 173.23  E-value: 1.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  27 AIVHLFEWRWVDIAKECERyLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKIC-SRSGNEDEFRDMVNRCNNVG 105
Cdd:cd11315    3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGnNQLGTEDDFKALCAAAHKYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 106 VRIYVDAVINHMCGVGAQAGqsstcgsyfNPNNRDFPGVPYSGFDFNDGKCrtasggIENYQDAAQVRDCRLSGLLDLAL 185
Cdd:cd11315   82 IKIIVDVVFNHMANEGSAIE---------DLWYPSADIELFSPEDFHGNGG------ISNWNDRWQVTQGRLGGLPDLNT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 186 EKDYVRTKVADYMNHLIDIGVAGFRLDASKHM-------WPGD-IKAILDKLHNLNtkwfsqgsrPFIFQEVidLGGEAV 257
Cdd:cd11315  147 ENPAVQQQQKAYLKALVALGVDGFRFDAAKHIelpdepsKASDfWTNILNNLDKDG---------LFIYGEV--LQDGGS 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 258 SSNEY---FGNGRVTEFKYGAKL-GKVMRKWDGEKMSYLKNWGEGwglMPSDRALVFVDNHDNQrGHGAGGASILTFWDA 333
Cdd:cd11315  216 RDSDYasyLSLGGVTASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY-NNDGFESTGLDDEDE 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 334 RlykMAVGFMLAHPYGftrvMSSYYWpRNFQNGKDvNDWVGPpnnngktkevsinpdstCGNDWICEHrwrQIRNMVAFR 413
Cdd:cd11315  292 R---LAWAYLAARDGG----TPLFFS-RPNGSGGT-NPQIGD-----------------RGDDAWKSP---DVVAVNKFH 342


                 ....*..
gi 160358819 414 NVVNGQP 420
Cdd:cd11315  343 NAMHGQP 349
Aamy_C smart00632
Aamy_C domain;
422-510 2.12e-32

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 118.49  E-value: 2.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   422 ANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISgdkvdGNCTGIKVYVGNDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 160358819   502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-121 2.95e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 107.42  E-value: 2.95e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819    28 IVHLFEWR-------WVDIAKECErYLAPNGFAGVQVSPPNENIVVhspsRPWWERYQPISYK-ICSRSGNEDEFRDMVN 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKqIDPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|..
gi 160358819   100 RCNNVGVRIYVDAVINHMCGVG 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 ...
 421-508 2.90e-18

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: 79.69  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  421 FANWWDNDSNQVAFGRGN---KGFIVFNNDDWALSETLQTGLP-AGTYCDVISGDKV--DGNCTGIKVYVGNDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEeyGGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 160358819  495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
82-347 6.87e-17

Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 82.60  E-value: 6.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHmCGVG------AQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGK 155
Cdd:COG0366   69 RDVDPRFGTLADFDELVAEAHARGIKVILDLVLNH-TSDEhpwfqeARAGPDSPYRDWYVWRDGKPDLPPNNWFSIFGGS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 156 CRTASGGIENYqdaaqVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKLH 230
Cdd:COG0366  148 AWTWDPEDGQY-----YLHLFFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLR 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 231 NLNTKWFSQGSRPFIFQEVIDLGGEAVSsnEYFGNGR---VTEFKYGAKLGKVMRKWDGEKM-SYLKNWGEgwgLMPSDR 306
Cdd:COG0366  223 ELRAAVDEYYPDFFLVGEAWVDPPEDVA--RYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPA---LYPEGG 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 160358819 307 ALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366  298 WWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-347 1.82e-16

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: 79.14  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  45 RYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYqpiSYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHmcgvgaqa 124
Cdd:cd00551   32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 125 gqsstcgsyfnpnnrdfpgvpysgfdfndgkcrtasggienyqdaaqvrdcrlsglldlalekdyvrtkvaDYMNHLIDI 204
Cdd:cd00551  101 -----------------------------------------------------------------------DILRFWLDE 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 205 GVAGFRLDASKHMWPGDIKAILDKLHNLNTKWfsqGSRPFIFQEVIDlGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKW 284
Cdd:cd00551  110 GVDGFRLDAAKHVPKPEPVEFLREIRKDAKLA---KPDTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFPLLEALRDALK 185

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160358819 285 DGEKMSYLKNWGEgWGLMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLyKMAVGFMLAHP 347
Cdd:cd00551  186 GGEGALAILAALL-LLNPEGALLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTLP 246
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-344 1.42e-12

Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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: 200459 [Multi-domain]  Cd Length: 389  Bit Score: 69.24  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  46 YLAPNGFAGVQVSPPNENIVVHSPSRPW------WER-YqpisYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMc 118
Cdd:cd11320   55 YLKDLGVTAIWISPPVENINSPIEGGGNtgyhgyWARdF----KRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHS- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 119 gvgaqagqsstcgsyfNPNNRDFPGVPY------SGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRT 192
Cdd:cd11320  130 ----------------SPADYAEDGALYdngtlvGDYPNDDNGWFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQ 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 193 KVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNlntkwfsqgSRP-FIFQEVIDLGGEAVSSNE-YFGNGR--- 267
Cdd:cd11320  194 YLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS---------KKPvFTFGEWFLGSPDPGYEDYvKFANNSgms 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160358819 268 VTEFKYGAKLGKVMRKwDGEKMSYLKNWGEGWG--LMPSDRALVFVDNHDNQRGHGAGGasiltfwDARLYKMAVGFML 344
Cdd:cd11320  265 LLDFPLNQAIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNN-------NDKRLHQALAFLL 335
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 2.78e-12

Alpha amylase, catalytic 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: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 67.77  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMcgvgaqagqsSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASG 161
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHT----------SDEHAWFQESRSSKDNPYRDYYFWRPGGGPIPPN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  162 GIENYQDAAQVRDCRLSG----------LLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDK--- 228
Cdd:pfam00128 112 NWRSYFGGSAWTYDEKGQeyylhlfvagQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNgpf 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  229 ----LHNLNTKWFSQGSRpFIFQEV-IDLGGEAV--SSNEYFGNGRVTEFKYGAKLGKVMRKWDGEK--MSYLKNWGEGW 299
Cdd:pfam00128 192 whefTQAMNETVFGYKDV-MTVGEVfHGDGEWARvyTTEARMELEMGFNFPHNDVALKPFIKWDLAPisARKLKEMITDW 270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 160358819  300 --GLMPSDRALV-FVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 271 ldALPDTNGWNFtFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 51-224 3.55e-12

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: 67.98  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  51 GFAGVQVSPPNENIVVHSPsrpWWERY-----QPIsYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMcgvgAQAG 125
Cdd:cd11319   56 GFDAIWISPIVKNIEGNTA---YGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM----ASAG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 126 QSSTcgsyfnpnnrdfpgVPYSGFD-FNDGK-----CRtasggIENYQDAAQVRDCRL----SGLLDLALEKDYVRTKVA 195
Cdd:cd11319  128 PGSD--------------VDYSSFVpFNDSSyyhpyCW-----ITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLN 188

                        170       180       190
                 ....*....|....*....|....*....|....
gi 160358819 196 DYMNHLI-DIGVAGFRLDASKHM----WPGDIKA 224
Cdd:cd11319  189 DWIKNLVsNYSIDGLRIDTAKHVrkdfWPGFVEA 222
PLN02784 PLN02784
alpha-amylase
 21-227 2.18e-08

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 56.94  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  21 TQYGRTAIVHLFEW------RWVDIAKECERYLAPNGFAGVQVSPPNENIvvhSPsrpwwERYQPIS-YKICSRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  94 FRDMVNRCNNVGVRIYVDAVINHMCG-VGAQAGQSSTCGSYFNPNNR----DFPgvpysgfDFNdGKCRTASGgiENYQD 168
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAhFQNQNGVWNIFGGRLNWDDRavvaDDP-------HFQ-GRGNKSSG--DNFHA 639

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 169 AAQVRDcrlsglldlalEKDYVRTKVADYMNHLID-IGVAGFRLDASKHMWPGDIKAILD 227
Cdd:PLN02784 640 APNIDH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYME 688
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-213 2.19e-07

Alpha amylase catalytic domain found in 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 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: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 52.71  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHmcgVGAQAgqsstcgSYFNPNNRDFPGVPYSGFDFNDGkcRTASG 161
Cdd:cd11354   67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNH---VGRSH-------PAVAQALEDGPGSEEDRWHGHAG--GGTPA 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160358819 162 GIENYQDaaqvrdcrlsgLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDA 213
Cdd:cd11354  135 VFEGHED-----------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDA 175
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 82-348 8.99e-07

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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 51.04  E-value: 8.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHmcgVGAQ------AGQSSTCG--SYFNPNNRDfpgvPYSGFDFND 153
Cdd:cd11316   60 YAIEPDYGTMEDFERLIAEAHKRGIKVIIDLVINH---TSSEhpwfqeAASSPDSPyrDYYIWADDD----PGGWSSWGG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 154 GKCRTASGGiENYQDAAQvrdcrlSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDiKAILDKLHNLN 233
Cdd:cd11316  133 NVWHKAGDG-GYYYGAFW------SGMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYENG-EGQADQEENIE 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 234 -TKWFSQ---GSRP--FIFQEVIDlGGEAVSsnEYFGNG--RVTEFKYGAKLGKVMRKW--DGEKMSYLKNW-GEGWGLM 302
Cdd:cd11316  205 fWKEFRDyvkSVKPdaYLVGEVWD-DPSTIA--PYYASGldSAFNFDLAEAIIDSVKNGgsGAGLAKALLRVyELYAKYN 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 160358819 303 PSDRALVFVDNHDNQRGHGAGGAsiltfwDARLYKMAVGFML---AHPY 348
Cdd:cd11316  282 PDYIDAPFLSNHDQDRVASQLGG------DEAKAKLAAALLLtlpGNPF 324
PRK14705 PRK14705
glycogen branching enzyme; Provisional
 15-116 3.37e-06

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 50.00  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819   15 AQYDPHTQYGRTAIVHLFEWR----WVDIAKECERYLAPNGFAGVQVSPPNEnivvHSPSRPWweRYQPISY-KICSRSG 89
Cdd:PRK14705  739 AERDPHNSPMSVYEVHLGSWRlglgYRELAKELVDYVKWLGFTHVEFMPVAE----HPFGGSW--GYQVTSYfAPTSRFG 812

                          90       100
                  ....*....|....*....|....*..
gi 160358819   90 NEDEFRDMVNRCNNVGVRIYVDAVINH 116
Cdd:PRK14705  813 HPDEFRFLVDSLHQAGIGVLLDWVPAH 839
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 82-332 9.69e-06

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: 47.60  E-value: 9.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  82 YKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGvgaqagqsstcgsyfnpnnrdfpgvPYSGFDFNdgkcrtasg 161
Cdd:cd11314   57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSG-------------------------PDTGEDFG--------- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 162 gienyqdAAQvrdcrlsgllDLALEKDYVRTKVADYMNHLI-DIGVAGFRLDASKHMWPGDIKAILDKLHN--------L 232
Cdd:cd11314  103 -------GAP----------DLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKGYAPSYVKEYNEATSPsfsvgeywD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 233 NTKWFSQGSRPFIFQEVIDLGG---------------EAVSSNEYFGngrvtefkygaklgkvMRKWDGEKMSYLKNWGE 297
Cdd:cd11314  166 GLSYENQDAHRQRLVDWIDATGggsaafdfttkyilqEAVNNNEYWR----------------LRDGQGKPPGLIGWWPQ 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160358819 298 gwglmpsdRALVFVDNHDNQRGHG----------AGGASILT-------FWD 332
Cdd:cd11314  230 --------KAVTFVDNHDTGSTQGhwpfptdnvlQGYAYILThpgtpcvFWD 273
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
 29-118 8.84e-05

Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme); The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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: 200461 [Multi-domain]  Cd Length: 402  Bit Score: 44.82  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  29 VHLFEWR---------WVDIAKECERYLAPNGFAGVQVSPPNENivvhsPSRPWWErYQPISY-KICSRSGNEDEFRDMV 98
Cdd:cd11322   41 VHLGSWKrkedgrflsYRELADELIPYVKEMGYTHVELMPVMEH-----PFDGSWG-YQVTGYfAPTSRYGTPDDFKYFV 114

                         90       100
                 ....*....|....*....|
gi 160358819  99 NRCNNVGVRIYVDAVINHMC 118
Cdd:cd11322  115 DACHQAGIGVILDWVPGHFP 134
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 182-351 1.18e-04

Alpha amylase catalytic domain found in 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 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: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 44.17  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 182 DLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHM----WPGDIKAILDKLHNLNTkwfsqgsrpFIFQEVIDLGGEAV 257
Cdd:cd11339  126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVprefWQEFAPAIRQAAGKPDF---------FMFGEVYDGDPSYI 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 258 SSNEYFGNG-RVTEFKYGAKLGKVMRKWDGekMSYLKNW-GEGWGLMPSDRALVFVDNHDNQRghgaggasILTFWDARL 335
Cdd:cd11339  197 APYTTTAGGdSVLDFPLYGAIRDAFAGGGS--GDLLQDLfLSDDLYNDATELVTFLDNHDMGR--------FLSSLKDGS 266

                        170
                 ....*....|....*.
gi 160358819 336 YKMAVGFMLAHPYGFT 351
Cdd:cd11339  267 ADGTARLALALALLFT 282
PLN02361 PLN02361
alpha-amylase
 22-332 2.13e-04

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 43.65  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  22 QYGRTAIVHLFEWR-----WVDIAKECERYLAPNGFAGVQVSPPNENIvvhSPsrpwwERYQPIS-YKICSRSGNEDEFR 95
Cdd:PLN02361   8 RNGREILLQAFNWEshkhdWWRNLEGKVPDLAKSGFTSAWLPPPSQSL---AP-----EGYLPQNlYSLNSAYGSEHLLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  96 DMVNRCNNVGVRIYVDAVINHMCGvgaqagqssTCGSYFNPNNRdFPGVPYSgfdFNDGKCRTASGGIENYQDAAQvrdc 175
Cdd:PLN02361  80 SLLRKMKQYNVRAMADIVINHRVG---------TTQGHGGMYNR-YDGIPLP---WDEHAVTSCTGGLGNRSTGDN---- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 176 rLSGLLDLALEKDYVRTKVADYMNHLI-DIGVAGFRLDASKHMWPGDIKAILDK---LHNLNTKW-------------FS 238
Cdd:PLN02361 143 -FNGVPNIDHTQHFVRKDIIGWLIWLRnDVGFQDFRFDFAKGYSAKFVKEYIEAakpLFSVGEYWdscnysgpdyrldYN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 239 QGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEfkygAKLGKVMRKWDGEkmsylknwGEGWGLM---PSdRALVFVDNHD 315
Cdd:PLN02361 222 QDSHRQRIVNWIDGTGGLSAAFDFTTKGILQE----AVKGQWWRLRDAQ--------GKPPGVMgwwPS-RAVTFIDNHD 288

                        330       340       350
                 ....*....|....*....|....*....|....
gi 160358819 316 --NQRGH--------GAGGASILT-------FWD 332
Cdd:PLN02361 289 tgSTQAHwpfpsdhiMEGYAYILThpgiptvFYD 322
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 89-217 2.86e-04

Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 43.27  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819  89 GNEDEFRDMVNRCNNVGVRIYVDAVINHMCGvgaqAGQSSTCGSY-FNPNNR----------------DFPGV--PYSGF 149
Cdd:cd11318   76 GTKEELLEAIKALHENGIQVYADAVLNHKAG----ADETETVKAVeVDPNDRnkeisepyeieawtkfTFPGRggKYSDF 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358819 150 ----------DFND-----GKCRTASGGIENYQDAAQvrdcrlsglldlalEK---DY------------VRTKVAD--- 196
Cdd:cd11318  152 kwnwqhfsgvDYDQktkkkGIFKINFEGKGWDEDVDD--------------ENgnyDYlmgadidysnpeVREELKRwgk 217

                        170       180
                 ....*....|....*....|..
gi 160358819 197 -YMNHLidiGVAGFRLDASKHM 217
Cdd:cd11318  218 wYINTT---GLDGFRLDAVKHI 236
 
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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