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Conserved domains on  [gi|157830769|pdb|1CYG|A]
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Protein Classification

AmyAc_AmyMalt_CGTase_like and CBM20_CGTase domain-containing protein (domain architecture ID 10183102)

protein containing domains AmyAc_AmyMalt_CGTase_like, Aamy_C, IPT_CGTD, and CBM20_CGTase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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  Cd Length: 389  Bit Score: 601.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320  79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320 153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320 233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CYG_A      324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320 313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 1.94e-60

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99882  Cd Length: 101  Bit Score: 200.09  E-value: 1.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                        90       100
                ....*....|....*....|.
1CYG_A      658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 1.74e-33

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


:

Pssm-ID: 238338  Cd Length: 81  Bit Score: 124.76  E-value: 1.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                ..
1CYG_A      575 LT 576
Cdd:cd00604  80 LT 81
Aamy_C smart00632
Aamy_C domain;
406-490 3.51e-17

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
1CYG_A         484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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  Cd Length: 389  Bit Score: 601.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320  79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320 153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320 233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CYG_A      324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320 313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
49-368 1.93e-85

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: 306608  Cd Length: 336  Bit Score: 275.39  E-value: 1.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         49 GDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:pfam00128   1 GDLQGIIDKLD--YLKGLGVTAIWLSPIFDS----------PQADHGYDIADYYKIDPHFGTMEDFKELISKAHEKGIKV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        129 IIDFAPNHTSPASE-TNPSYMENGRLYDNGTLLGG---YTNDANMYFhHNGGTTFS----SLEDGIYRNLFDLADLNHQN 200
Cdd:pfam00128  69 ILDLVFNHTSDEHAwFQESRKSKGNPYRDYYFWRPggtPIPPNNWRS-VFGGSAWTydewGQEYYLHLFAASQPDLNWEN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        201 PVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPF--------GWQKSLMDEIDNY----RPVFTFGEWFLSENE---VDANN 265
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVNHVSKvpglenngPFWHEFTQAMNETkfsyKDVMTVGEVWGDAGEdarVYTTE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        266 HYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAY-DEVLDQVTFIDNHDMDRFMIDGGDPR-----KVD 339
Cdd:pfam00128 228 AVMELEMGFNFPHFDVALKPFIKWQLNPISARKLKEMLTDWLDALpDTNGWNFTFLGNHDQPRFLSRFGDDRayrekKAK 307
                         330       340
                  ....*....|....*....|....*....
1CYG_A        340 MALAVLLTSRGVPNIYYGTEQYMTGNGDP 368
Cdd:pfam00128 308 LAAILLLTLPGTPYIYQGEEIGMTGGNDP 336
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 1.94e-60

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99882  Cd Length: 101  Bit Score: 200.09  E-value: 1.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                        90       100
                ....*....|....*....|.
1CYG_A      658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
AmyA COG0366
Glycosidase [Carbohydrate transport and metabolism];
13-433 1.12e-52

Glycosidase [Carbohydrate transport and metabolism];


Pssm-ID: 223443  Cd Length: 505  Bit Score: 190.97  E-value: 1.12e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNPSgalfssgctnlrKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfsvmndasgsAS 92
Cdd:COG0366   2 VIYQIYPDRFADSNGSNGPD------------YDGGGDLKGITEKL--DYLKELGVDAIWLSPIFESP----------QA 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNG-----TLLGGYTNDA 167
Cdd:COG0366  58 DHGYDVSDYTKVDPHFGTEEDFKELVEEAHKRGIKVILDLVFNHTSDEHPWFKEARSSKPNPKRSdyyiwRDPDPDGTPP 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      168 NMYFHHNGGTTFSSLEDG-IYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM--PFG--------- 233
Cdd:COG0366 138 NNWFSVFGGDAWTWGNTGeYYLHLFSseQPDLNWENPEVREELLDVVKFWLDKGVDGFRLDAAKHIskDFGlppseenlt 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      234 --------WQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNWYGFNQMIQD 305
Cdd:COG0366 218 fleeiheyLREENPDVLIYGEAITDVGEAPGAVKEDFADNTSFTNPELSMLFDFSHVGLDFEALAPL--DAEELKEILAD 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      306 TASAYDEVLDQ-VTFIDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMS---- 375
Cdd:COG0366 296 WPLAVNLNDGWnNLFLSNHDQPRLLsrfgdDVGGRDASAKLLAALLFLLPGTPFIYYGDELGLTNFKDPPIKYYDDveld 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      376 -----------------------SFNKNTRA-------------------------YQVIQKLSSLRR-NNPALAYGDTE 406
Cdd:COG0366 376 siillsrdgcrtpmpwdenglnaGFTGGKPWlsvnpndllginveaqladelpeslFNFYRRLIALRKqHSALLANGEDF 455
                       490       500
                ....*....|....*....|....*....
1CYG_A      407 QRWINGD--VYVYERQFGKDVVLVAVNRS 433
Cdd:COG0366 456 VLLADDDpsLLAFLRESGGETLLVVNNLS 484
CBM_20 pfam00686
Starch binding domain;
580-676 1.10e-37

Starch binding domain;


Pssm-ID: 307023  Cd Length: 96  Bit Score: 136.67  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:pfam00686   1 VPVTFNVN-ATTQYGQNVYIVGSIPELGNWNPKKAVALSASEYTSSYPLWSGTVDLPAGTTIEYKYIKKDSDGNVTWESG 79
                          90
                  ....*....|....*..
1CYG_A        660 SNHVYTTPTNTTGKIIV 676
Cdd:pfam00686  80 PNRSYTVPASGQGTTTT 96
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
13-436 1.15e-37

maltodextrin glucosidase; Provisional


Pssm-ID: 236759  Cd Length: 598  Bit Score: 148.23  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        13 VVYQIVVDRFVDGNTSNN-PSGALF--SSGCTNLRK--------------YCGGDWQGIINKIndGYLTDMGVTAIWISq 75
Cdd:PRK10785 123 VFYQIFPDRFARSLPREAvQDHVYYhhAAGQEIILRdwdepvtaqaggstFYGGDLDGISEKL--PYLKKLGVTALYLN- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        76 PVenvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasETNPSYMENGRlyd 155
Cdd:PRK10785 200 PI---FT-------APSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG---DSHPWFDRHNR--- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       156 ngTLLGGYTNDA----NMYFHHNGGTTFSSLedGIYrnlfDLADLNHQNP-VIDR-YLKD--AVKMWID--MGIDGIRMD 225
Cdd:PRK10785 264 --GTGGACHHPDspwrDWYSFSDDGRALDWL--GYA----SLPKLDFQSEeVVNEiYRGEdsIVRHWLKapYNIDGWRLD 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       226 AVkHM-------------------------P--------FG----W-QKSLMDEIDNYRPvFTFGEW-FLSENEVDANNH 266
Cdd:PRK10785 336 VV-HMlgegggarnnlqhvagitqaakeenPeayvlgehFGdarqWlQADVEDAAMNYRG-FAFPLRaFLANTDIAYHPQ 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       267 YFANESGMSLLD-FR----FGQKLRQvlrnnsdnwygFNQMiqdtasaydevldqvtfiDNHDMDRFM-IDGGDPRKVDM 340
Cdd:PRK10785 414 QIDAQTCAAWMDeYRaglpHQQQLRQ-----------FNQL------------------DSHDTARFKtLLGGDKARMPL 464
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       341 ALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM----SSFNKNTRAYqvIQKLSSLRRNNPALAYGDTEQRWINGDVYV 416
Cdd:PRK10785 465 ALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFpwdeAKQDGALLAL--YQRMIALRKKSQALRRGGCQVLYAEGNVVV 542
                        490       500
                 ....*....|....*....|
1CYG_A       417 YERQFGKDVVLVAVNRSSSS 436
Cdd:PRK10785 543 FARVLQQQRVLVAINRGEAC 562
Aamy smart00642
Alpha-amylase domain;
16-139 1.19e-37

Alpha-amylase domain;


Pssm-ID: 214758  Cd Length: 166  Bit Score: 139.00  E-value: 1.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A          16 QIVVDRFVDGNTSNnpsgalfssgctnlrkycGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSASYHG 95
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESP-------QGYPSYHG 53
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
1CYG_A          96 YWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:smart00642  54 YDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 1.74e-33

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


Pssm-ID: 238338  Cd Length: 81  Bit Score: 124.76  E-value: 1.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                ..
1CYG_A      575 LT 576
Cdd:cd00604  80 LT 81
CBM_2 smart01065
Starch binding domain;
580-668 2.52e-27

Starch binding domain;


Pssm-ID: 215006  Cd Length: 88  Bit Score: 107.82  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgPMfNQVVYSYPTWYIDVSVPE-GKTIEFKFIKKDSQGNVTWES 658
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPPaGTTIEYKYVKVDEDGSVTWES 78
                           90
                   ....*....|
1CYG_A         659 GSNHVYTTPT 668
Cdd:smart01065  79 GPNRRLTVPE 88
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
8-369 6.12e-23

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115  Cd Length: 543  Bit Score: 103.19  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A          8 NFTSDVVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKINdgYLTDMGVTAIWISqPVenVFSVMNDa 87
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGT------------------GDLRGIIEKLD--YLKKLGVDYIWLN-PF--YVSPQKD- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         88 sgsasyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-------PASETNPSYM-------ENGRL 153
Cdd:TIGR02403  57 ------NGYDVSDYYAINPLFGTMADFEELVSEAKKRNIKIMLDMVFNHTStehewfkKALAGDSPYRdfyiwrdPKGKP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        154 YDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLFDL--ADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDa 226
Cdd:TIGR02403 131 PTNwQSKFGGsaweYFGDTGQYYLH----------------LFDKtqADLNWENPEVREELKDVVNFWRDKGVDGFRLD- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        227 VKHMPFGWQKSLMDEIDNYRPVFTFG---EWFLSEnevdANNHYFANESGMSL---------------------LDFRFG 282
Cdd:TIGR02403 194 VINLISKDQFFEDDEIGDGRRFYTDGprvHEYLQE----MNQEVFGDNDSVTVgemssttiencirysnpenkeLSMVFT 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        283 QKLRQVLRNNSDNW----YGFNQM--IQDTASAYDEVLD--QVTFIDNHDMDRFMIDGGDPRK-----VDMALAVLLTSR 349
Cdd:TIGR02403 270 FHHLKVDYPNGEKWtlakFDFAKLkeIFSTWQTGMQAGGgwNALFWNNHDQPRAVSRFGDDGEyrvesAKMLAAAIHLLR 349
                         410       420
                  ....*....|....*....|
1CYG_A        350 GVPNIYYGTEQYMTGNGDPN 369
Cdd:TIGR02403 350 GTPYIYQGEEIGMTNPKFTN 369
Aamy_C smart00632
Aamy_C domain;
406-490 3.51e-17

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
1CYG_A         484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
495-573 4.14e-08

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 307788  Cd Length: 85  Bit Score: 52.47  E-value: 4.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        495 PIIGHVGPMMGQV--GHQVTIDGEGFGTNTG--TVKFGTTAANVV-SWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAY 569
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdtKVTIGGTPCTVIaSVSSTTIVCTTPPGTSGLVNVSVTVGGGGLSSSN 80

                  ....
1CYG_A        570 DNFE 573
Cdd:pfam01833  81 LTFT 84
PLN02950 PLN02950
4-alpha-glucanotransferase
572-663 3.64e-05

4-alpha-glucanotransferase


Pssm-ID: 215512  Cd Length: 909  Bit Score: 47.02  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       572 FEVLTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKaiGPMFNQVVysYPTWYIDVSVPEGK-TIEFKFIKKDS 650
Cdd:PLN02950 145 NKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDD--GLKLNYTG--DSIWEADCLVPKSDfPIKYKYALQTA 220
                         90
                 ....*....|...
1CYG_A       651 QGNVTWESGSNHV 663
Cdd:PLN02950 221 EGLVSLELGVNRE 233
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
409-489 3.89e-04

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: 308448  Cd Length: 92  Bit Score: 40.38  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        409 WINGD-----VYVYERqfgKDVVLVAVNRSSSSNYsiTGLFTALP-AGTYTDQL--------GGLLDGNTIQVGSNGSVN 474
Cdd:pfam02806   1 WIDGDdaennVIAFER---GDKLLVVFNFTPSVSY--TDYRTGVPlAGTYCEVLntddeeygGSGNTGEVVTVDGPGHAN 75
                          90
                  ....*....|....*..
1CYG_A        475 A--FDLGPGEVGVWAYS 489
Cdd:pfam02806  76 SltLTLPPLSALVLKVE 92
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
8-396 0e+00

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  Cd Length: 389  Bit Score: 601.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        8 NFTSDVVYQIVVDRFVDGNTSNNPSG--ALFSSGCTNLRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVFSVMN 85
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       86 DAsGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetnpsYMENGRLYDNGTLLGGYTN 165
Cdd:cd11320  79 GG-GNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD-----YAEDGALYDNGTLVGDYPN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      166 DANMYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN 244
Cdd:cd11320 153 DDNGWFHHNGGIDdWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      245 YRPVFTFGEWFL-SENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11320 233 KKPVFTFGEWFLgSPDPGYEDYVKFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNH 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CYG_A      324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGN----GDPNNRKMMSSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11320 313 DMPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGGtqvgGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
10-397 2.21e-88

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  Cd Length: 344  Bit Score: 283.38  E-value: 2.21e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       10 TSDVVYQIVVDRFVDGNTSNNPSGA--LFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvMNDA 87
Cdd:cd11339   1 REETIYFVMTDRFYDGDPSNDNGGGdgDPRSNPTDNGPYHGGDFKGLIDKLD--YIKDLGFTAIWITPVVKN----RSVQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       88 SGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasetnpsymengrlydngtllggytnda 167
Cdd:cd11339  75 AGSAGYHGYWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG----------------------------- 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      168 nmyfhhnggttfssledgiyrnlfdlaDLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDN--- 244
Cdd:cd11339 126 ---------------------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQaag 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      245 YRPVFTFGEWFLSENEVDANnhYFANESGMSLLDFRFGQKLRQVLRNNS-----DNWYGFNQMIQDTASaydevldQVTF 319
Cdd:cd11339 179 KPDFFMFGEVYDGDPSYIAP--YTTTAGGDSVLDFPLYGAIRDAFAGGGsgdllQDLFLSDDLYNDATE-------LVTF 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      320 IDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM------------SSFNKNTR 382
Cdd:cd11339 250 LDNHDMGRFLsslkdGSADGTARLALALALLFTSRGIPCIYYGTEQGFTGGGDPDNGRRNmfastgdltsadDNFDTDHP 329
                       410
                ....*....|....*
1CYG_A      383 AYQVIQKLSSLRRNN 397
Cdd:cd11339 330 LYQYIARLNRIRRAY 344
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
49-368 1.93e-85

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: 306608  Cd Length: 336  Bit Score: 275.39  E-value: 1.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         49 GDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:pfam00128   1 GDLQGIIDKLD--YLKGLGVTAIWLSPIFDS----------PQADHGYDIADYYKIDPHFGTMEDFKELISKAHEKGIKV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        129 IIDFAPNHTSPASE-TNPSYMENGRLYDNGTLLGG---YTNDANMYFhHNGGTTFS----SLEDGIYRNLFDLADLNHQN 200
Cdd:pfam00128  69 ILDLVFNHTSDEHAwFQESRKSKGNPYRDYYFWRPggtPIPPNNWRS-VFGGSAWTydewGQEYYLHLFAASQPDLNWEN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        201 PVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPF--------GWQKSLMDEIDNY----RPVFTFGEWFLSENE---VDANN 265
Cdd:pfam00128 148 PEVRNELYDVVRFWLDKGIDGFRIDVVNHVSKvpglenngPFWHEFTQAMNETkfsyKDVMTVGEVWGDAGEdarVYTTE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        266 HYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAY-DEVLDQVTFIDNHDMDRFMIDGGDPR-----KVD 339
Cdd:pfam00128 228 AVMELEMGFNFPHFDVALKPFIKWQLNPISARKLKEMLTDWLDALpDTNGWNFTFLGNHDQPRFLSRFGDDRayrekKAK 307
                         330       340
                  ....*....|....*....|....*....
1CYG_A        340 MALAVLLTSRGVPNIYYGTEQYMTGNGDP 368
Cdd:pfam00128 308 LAAILLLTLPGTPYIYQGEEIGMTGGNDP 336
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
11-396 9.66e-68

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: 200479  Cd Length: 407  Bit Score: 230.18  E-value: 9.66e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       11 SDVVYQIVVDRFVDGNTSN-NPSGALFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENvfsvmndASG 89
Cdd:cd11340   3 SDVIYLIMPDRFANGDPSNdSVPGMLEKADRSNPNGRHGGDIQGIIDHLD--YLQDLGVTAIWLTPLLEN-------DMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       90 SASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAsetNPsYMENGRLYD--NGTLLGGYTNda 167
Cdd:cd11340  74 SYSYHGYAATDFYRIDPRFGSNEDYKELVSKAHARGMKLIMDMVPNHCGSE---HW-WMKDLPTKDwiNQTPEYTQTN-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      168 nmyfhHNggttFSSLEDgIY------RNLFD------LADLNHQNPVIDRYLKDAVKMWIDM-GIDGIRMD----AVKHM 230
Cdd:cd11340 148 -----HR----RTALQD-PYasqadrKLFLDgwfvptMPDLNQRNPLVARYLIQNSIWWIEYaGLDGIRVDtypySDKDF 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      231 PFGWQKSLMDEIDNYrpvFTFGE-WFLSENEV----DANNHYFANESGM-SLLDFRFGQKLRQVLrnNSDNWYG------ 298
Cdd:cd11340 218 MSEWTKAIMEEYPNF---NIVGEeWSGNPAIVaywqKGKKNPDGYDSHLpSVMDFPLQDALRDAL--NEEEGWDtglnrl 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      299 FNQMIQDtaSAYDEVLDQVTFIDNHDMDRFM-IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTG---NGDPNNRKMM 374
Cdd:cd11340 293 YETLAND--FLYPDPNNLVIFLDNHDTSRFYsQVGEDLDKFKLALALLLTTRGIPQLYYGTEILMKGtkkKDDGAIRRDF 370
                       410       420       430
                ....*....|....*....|....*....|....*..
1CYG_A      375 ---------SSFNKNTR------AYQVIQKLSSLRRN 396
Cdd:cd11340 371 pggwagdkvNAFTAAGRtpeqneAFDFVRKLLNWRKN 407
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
13-396 9.76e-64

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  Cd Length: 375  Bit Score: 218.59  E-value: 9.76e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNPSgalfssgCTNL-RKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVFSvmNDASGSA 91
Cdd:cd11319  10 SIYQVLTDRFARTDGSSTAP-------CDTAdRTYCGGTWKGIINKLD--YIQGMGFDAIWISPIVKNIEG--NTAYGEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       92 sYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGTllggytndanmYF 171
Cdd:cd11319  79 -YHGYWAQDLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDYSSFVPFNDSS-----------YY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      172 HH----NGGTTFSSLEDG-IYRNLFDLADLNHQNPVIDRYLKDAVKMWI-DMGIDGIRMDAVKHMPFGWQKSLMDEIDny 245
Cdd:cd11319 147 HPycwiTDYNNQTSVEDCwLGDDVVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVRKDFWPGFVEAAG-- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      246 rpVFTFGEWFlsenevDANNHYFAN--ESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:cd11319 225 --VFAIGEVF------DGDPNYVCPyqNYLDGVLNYPLYYPLVDAFQSTKGSMSALVDTINSVQSSCKDPTLLGTFLENH 296
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1CYG_A      324 DMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM--SSFNKNTRAYQVIQKLSSLRRN 396
Cdd:cd11319 297 DNPRFLSYTSDQALAKNALAFTLLSDGIPIIYYGQEQGFNGGNDPYNREALwlSGYDTSSPLYKFIKTLNAIRKA 371
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
13-404 1.66e-61

Alpha amylase catalytic domain found in 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). 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: 200477  Cd Length: 389  Bit Score: 212.73  E-value: 1.66e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYC--------------GGDWQGIINKIndGYLTDMGVTAIWISqPVe 78
Cdd:cd11338   3 VFYQIFPDRFANGDPSNDPKGGEYNYFGWPDLPDYpppwggeptrrdfyGGDLQGIIEKL--DYLKDLGVNAIYLN-PI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       79 nvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRlydngt 158
Cdd:cd11338  79 --FE-------APSNHKYDTADYFKIDPHLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLKYGE------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      159 lLGGYtndaNMYFHHNGGTTFSSLEDGIYR---NLFDLADLNHQNPVIDRYLKDAVKMWIDMG-IDGIRMDAVKHMPFGW 234
Cdd:cd11338 144 -SSAY----QDWFSIYYFWPYFTDEPPNYEswwGVPSLPKLNTENPEVREYLDSVARYWLKEGdIDGWRLDVADEVPHEF 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      235 QKSLMDEIDNYRP-VFTFGE-W-----FLSENEVDAN-NHYFANesgmSLLDFrfgqklrqvLRNNSDNWYGFNQMIQDT 306
Cdd:cd11338 219 WREFRKAVKAVNPdAYIIGEvWedarpWLQGDQFDSVmNYPFRD----AVLDF---------LAGEEIDAEEFANRLNSL 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      307 ASAY-DEVLD-QVTFIDNHDMDRFM-IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM--SSFNKNT 381
Cdd:cd11338 286 RANYpKQVLYaMMNLLDSHDTPRILtLLGGDKARLKLALALQFTLPGAPCIYYGDEIGLEGGKDPDNRRPMpwDEEKWDQ 365
                       410       420
                ....*....|....*....|...
1CYG_A      382 RAYQVIQKLSSLRRNNPALAYGD 404
Cdd:cd11338 366 DLLEFYKKLIALRKEHPALRTGG 388
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
578-678 1.94e-60

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99882  Cd Length: 101  Bit Score: 200.09  E-value: 1.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      578 DQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWE 657
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80
                        90       100
                ....*....|....*....|.
1CYG_A      658 SGSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
12-403 3.73e-55

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  Cd Length: 403  Bit Score: 195.49  E-value: 3.73e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       12 DVVYQIVVDRFVDGNtsnnpsgalfssgctnlrkycG---GDWQGIINKINdgYLTDMGVTAIWISqPVenvfsvmndaS 88
Cdd:cd11316   1 GVFYEIFVRSFYDSD---------------------GdgiGDLNGLTEKLD--YLNDLGVNGIWLM-PI----------F 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       89 GSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P-----ASETNPSYmengRLY-----D 155
Cdd:cd11316  47 PSPSYHGYDVTDYYAIEPDYGTMEDFERLIAEAHKRGIKVIIDLVINHTSsehPwfqeaASSPDSPY----RDYyiwadD 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      156 NGTLLGGYtnDANMYFHHNGGttfssledGIYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFG 233
Cdd:cd11316 123 DPGGWSSW--GGNVWHKAGDG--------GYYYGAFWsgMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYEN 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      234 ------------WQKSLMDEIDNYRP-VFTFGEWFLSENEVDAnnhYFANESGmSLLDFRFGQKLRQVLRNNSDNwYGFN 300
Cdd:cd11316 193 gegqadqeenieFWKEFRDYVKSVKPdAYLVGEVWDDPSTIAP---YYASGLD-SAFNFDLAEAIIDSVKNGGSG-AGLA 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      301 QMIQDTASAYDEVLDQV---TFIDNHDMDRFMID-GGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNG-DPNNRKMMS 375
Cdd:cd11316 268 KALLRVYELYAKYNPDYidaPFLSNHDQDRVASQlGGDEAKAKLAAALLLTLPGNPFIYYGEEIGMLGSKpDENIRTPMS 347
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
1CYG_A      376 -----------------SFNKNTRA-----------YQVIQKLSSLRRNNPALAYG 403
Cdd:cd11316 348 wdadsgagfttwipprpNTNATTASveaqeadpdslLNHYKRLIALRNEYPALARG 403
AmyA COG0366
Glycosidase [Carbohydrate transport and metabolism];
13-433 1.12e-52

Glycosidase [Carbohydrate transport and metabolism];


Pssm-ID: 223443  Cd Length: 505  Bit Score: 190.97  E-value: 1.12e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNPSgalfssgctnlrKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfsvmndasgsAS 92
Cdd:COG0366   2 VIYQIYPDRFADSNGSNGPD------------YDGGGDLKGITEKL--DYLKELGVDAIWLSPIFESP----------QA 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNG-----TLLGGYTNDA 167
Cdd:COG0366  58 DHGYDVSDYTKVDPHFGTEEDFKELVEEAHKRGIKVILDLVFNHTSDEHPWFKEARSSKPNPKRSdyyiwRDPDPDGTPP 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      168 NMYFHHNGGTTFSSLEDG-IYRNLFD--LADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM--PFG--------- 233
Cdd:COG0366 138 NNWFSVFGGDAWTWGNTGeYYLHLFSseQPDLNWENPEVREELLDVVKFWLDKGVDGFRLDAAKHIskDFGlppseenlt 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      234 --------WQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNWYGFNQMIQD 305
Cdd:COG0366 218 fleeiheyLREENPDVLIYGEAITDVGEAPGAVKEDFADNTSFTNPELSMLFDFSHVGLDFEALAPL--DAEELKEILAD 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      306 TASAYDEVLDQ-VTFIDNHDMDRFM-----IDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMS---- 375
Cdd:COG0366 296 WPLAVNLNDGWnNLFLSNHDQPRLLsrfgdDVGGRDASAKLLAALLFLLPGTPFIYYGDELGLTNFKDPPIKYYDDveld 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      376 -----------------------SFNKNTRA-------------------------YQVIQKLSSLRR-NNPALAYGDTE 406
Cdd:COG0366 376 siillsrdgcrtpmpwdenglnaGFTGGKPWlsvnpndllginveaqladelpeslFNFYRRLIALRKqHSALLANGEDF 455
                       490       500
                ....*....|....*....|....*....
1CYG_A      407 QRWINGD--VYVYERQFGKDVVLVAVNRS 433
Cdd:COG0366 456 VLLADDDpsLLAFLRESGGETLLVVNNLS 484
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
13-393 5.09e-49

Alpha amylase catalytic domain found in an uncharacterized protein 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; 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: 200489  Cd Length: 443  Bit Score: 179.05  E-value: 5.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDG-------NTSNNPSGALFSSGCTN---LRKYCGGDWQGIINKIndGYLTDMGVTAIWISQPVENVfs 82
Cdd:cd11352   1 VLYFLLVDRFSDGkerprplFDGNDPAVATWEDNFGWesqGQRFQGGTLKGVRSKL--GYLKRLGVTALWLSPVFKQR-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       83 vmndaSGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-----PASETNPSYME---NGRLY 154
Cdd:cd11352  77 -----PELETYHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGdvfsyDDDRPYSSSPGyyrGFPNY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      155 DNGTLLGGYTNDANMYFHHNGG---------TTFS-----SLEDG----IYRNLFDLADLNHQNPVID----RYLKDAVK 212
Cdd:cd11352 152 PPGGWFIGGDQDALPEWRPDDAiwpaelqnlEYYTrkgriRNWDGypeyKEGDFFSLKDFRTGSGSIPsaalDILARVYQ 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      213 MWI---DmgIDGIRMDAVKHMPFGWQKSLMDEIDNY------RPVFTFGEWflsenevdANNHYFANESGMSL------L 277
Cdd:cd11352 232 YWIayaD--IDGFRIDTVKHMEPGAARYFCNAIKEFaqsigkDNFFLFGEI--------TGGREAAAYEDLDVtgldaaL 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      278 DFRFGQ-KLRQVLRNNSD-NWY--GFNQMIQDTASAYDEVLDQ-VTFIDNHDM------DRFMIDGGDPRKVDMALAVLL 346
Cdd:cd11352 302 DIPEIPfKLENVAKGLAPpAEYfqLFENSKLVGMGSHRWYGKFhVTFLDDHDQvgrfykKRRAADAAGDAQLAAALALNL 381
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1CYG_A      347 TSRGVPNIYYGTEQYMTGNGD---------------PNNRKMMSSFNKNTRAYQVIQKLSSL 393
Cdd:cd11352 382 FTLGIPCIYYGTEQGLDGSGDsdryvreamfggdfgAFRSRGRHFFNEEHPIYRRIAALSEL 443
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
13-356 2.88e-46

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  Cd Length: 260  Bit Score: 166.19  E-value: 2.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSAS 92
Cdd:cd00551   1 VIYQLFPDRFTDGDSSGG---------------DGGGDLKGIIDKLD--YLKDLGVTAIWLTPIFESP-------EYDGY 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       93 YHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHtspasetnpsymengrlydngtllggytndanmyfh 172
Cdd:cd00551  57 DKDDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH------------------------------------ 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      173 hnggttfssledgiyrnlfdladlnhqnpVIDRYlkdavkmWIDMGIDGIRMDAVKHMPFGWQKSLMDEI-----DNYRP 247
Cdd:cd00551 101 -----------------------------DILRF-------WLDEGVDGFRLDAAKHVPKPEPVEFLREIrkdakLAKPD 144
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      248 VFTFGEWFlsENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDtasaYDEVLDQVTFIDNHDMDR 327
Cdd:cd00551 145 TLLLGEAW--GGPDELLAKAGFDDGLDSVFDFPLLEALRDALKGGEGALAILAALLLL----NPEGALLVNFLGNHDTFR 218
                       330       340       350
                ....*....|....*....|....*....|....*
1CYG_A      328 FM------IDGGDPRKVDMALAVLLTSRGVPNIYY 356
Cdd:cd00551 219 LAdlvsykIVELRKARLKLALALLLTLPGTPMIYY 253
CBM_20 pfam00686
Starch binding domain;
580-676 1.10e-37

Starch binding domain;


Pssm-ID: 307023  Cd Length: 96  Bit Score: 136.67  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:pfam00686   1 VPVTFNVN-ATTQYGQNVYIVGSIPELGNWNPKKAVALSASEYTSSYPLWSGTVDLPAGTTIEYKYIKKDSDGNVTWESG 79
                          90
                  ....*....|....*..
1CYG_A        660 SNHVYTTPTNTTGKIIV 676
Cdd:pfam00686  80 PNRSYTVPASGQGTTTT 96
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
42-403 1.12e-37

Alpha amylase catalytic domain found in archaeal and 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, bacteroidetes, and proteobacteria. 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: 200452  Cd Length: 336  Bit Score: 143.84  E-value: 1.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       42 NLRKYCG-GDWQGIINKIndGYLTDMGVTAIWIS--QPVenvfSVMNDASGSASYhgYWARDFKKPNPFFGTLSDFQRLV 118
Cdd:cd11313  11 NVRQFTPeGTFKAVTKDL--PRLKDLGVDILWLMpiHPI----GEKNRKGSLGSP--YAVKDYRAVNPEYGTLEDFKALV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      119 DAAHAKGIKVIIDFAPNHTSPASETNPSYMEngrlydngtllggytndanmYFHHNggttfsslEDGIYRNLF----DLA 194
Cdd:cd11313  83 DEAHDRGMKVILDWVANHTAWDHPLVEEHPE--------------------WYLRD--------SDGNITNKVfdwtDVA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      195 DLNHQNPVIDRYLKDAVKMWIDM-GIDGIRMDAVKHMPFGWQKSLMDEIDNYRP-VFTFGEW-----FLSENEVDAnnHY 267
Cdd:cd11313 135 DLDYSNPELRDYMIDAMKYWVREfDVDGFRCDVAWGVPLDFWKEARAELRAVKPdVFMLAEAeprddDELYSAFDM--TY 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      268 fanesgmsllDFRFGQKLRQVLRNNSDnwygfnqmiqdtASAYDEVLDQ-----------VTFIDNHDMDRFMIDGGDPR 336
Cdd:cd11313 213 ----------DWDLHHTLNDVAKGKAS------------ASDLLDALNAqeagypknavkMRFLENHDENRWAGTVGEGD 270
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1CYG_A      337 KVDMALAVLLTSRGVPNIYYGTEQYMTG-----NGDPnnrkmmSSFNKNTRAYQVIQKLSSLRRNNPALAYG 403
Cdd:cd11313 271 ALRAAAALSFTLPGMPLIYNGQEYGLDKrpsffEKDP------IDWTKNHDLTDLYQKLIALKKENPALRGG 336
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
13-436 1.15e-37

maltodextrin glucosidase; Provisional


Pssm-ID: 236759  Cd Length: 598  Bit Score: 148.23  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        13 VVYQIVVDRFVDGNTSNN-PSGALF--SSGCTNLRK--------------YCGGDWQGIINKIndGYLTDMGVTAIWISq 75
Cdd:PRK10785 123 VFYQIFPDRFARSLPREAvQDHVYYhhAAGQEIILRdwdepvtaqaggstFYGGDLDGISEKL--PYLKKLGVTALYLN- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        76 PVenvFSvmndasgSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpasETNPSYMENGRlyd 155
Cdd:PRK10785 200 PI---FT-------APSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRGMRLVLDGVFNHTG---DSHPWFDRHNR--- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       156 ngTLLGGYTNDA----NMYFHHNGGTTFSSLedGIYrnlfDLADLNHQNP-VIDR-YLKD--AVKMWID--MGIDGIRMD 225
Cdd:PRK10785 264 --GTGGACHHPDspwrDWYSFSDDGRALDWL--GYA----SLPKLDFQSEeVVNEiYRGEdsIVRHWLKapYNIDGWRLD 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       226 AVkHM-------------------------P--------FG----W-QKSLMDEIDNYRPvFTFGEW-FLSENEVDANNH 266
Cdd:PRK10785 336 VV-HMlgegggarnnlqhvagitqaakeenPeayvlgehFGdarqWlQADVEDAAMNYRG-FAFPLRaFLANTDIAYHPQ 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       267 YFANESGMSLLD-FR----FGQKLRQvlrnnsdnwygFNQMiqdtasaydevldqvtfiDNHDMDRFM-IDGGDPRKVDM 340
Cdd:PRK10785 414 QIDAQTCAAWMDeYRaglpHQQQLRQ-----------FNQL------------------DSHDTARFKtLLGGDKARMPL 464
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       341 ALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMM----SSFNKNTRAYqvIQKLSSLRRNNPALAYGDTEQRWINGDVYV 416
Cdd:PRK10785 465 ALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFpwdeAKQDGALLAL--YQRMIALRKKSQALRRGGCQVLYAEGNVVV 542
                        490       500
                 ....*....|....*....|
1CYG_A       417 YERQFGKDVVLVAVNRSSSS 436
Cdd:PRK10785 543 FARVLQQQRVLVAINRGEAC 562
Aamy smart00642
Alpha-amylase domain;
16-139 1.19e-37

Alpha-amylase domain;


Pssm-ID: 214758  Cd Length: 166  Bit Score: 139.00  E-value: 1.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A          16 QIVVDRFVDGNTSNnpsgalfssgctnlrkycGGDWQGIINKINdgYLTDMGVTAIWISQPVENVfsvmndaSGSASYHG 95
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESP-------QGYPSYHG 53
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
1CYG_A          96 YWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:smart00642  54 YDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTSD 97
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
62-405 1.76e-35

Alpha amylase catalytic domain found in 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: 200476  Cd Length: 328  Bit Score: 137.66  E-value: 1.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAIWISqPVenvFSvmndasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTspas 141
Cdd:cd11337  36 HLKELGCNALYLG-PV---FE--------SDSHGYDTRDYYRIDRRLGTNEDFKALVAALHERGIRVVLDGVFNHV---- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      142 etnpsymenGRlydnGTLLGGYtndanmyfhhnggttfssledgiyrnlFDLADLNHQNPVIDRYLKDAVKMWIDMG-ID 220
Cdd:cd11337 100 ---------GR----DFFWEGH---------------------------YDLVKLNLDNPAVVDYLFDVVRFWIEEFdID 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      221 GIRMDAVKHMPFGWQKSLMDEIDNYRPVFtfgeWFLSEneV---DANnhYFANESGM--------------SLLDFRFGQ 283
Cdd:cd11337 140 GLRLDAAYCLDPDFWRELRPFCRELKPDF----WLMGE--VihgDYN--RWVNDSMLdsvtnyelykglwsSHNDHNFFE 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      284 --KLRQVLRNNSDNWYGFNQMiqdtasaydevldqvTFIDNHDMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQY 361
Cdd:cd11337 212 iaHSLNRLFRHNGLYRGFHLY---------------TFVDNHDVTRIASILGDKAHLPLAYALLFTMPGIPSIYYGSEWG 276
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
1CYG_A      362 MTG---NGDPNNRKMM-----SSFNKNTRAYQVIQKLSSLRRNNPALAYGDT 405
Cdd:cd11337 277 IEGvkeEGSDADLRPLplrpaELSPLGNELTRLIQALIALRRRSPALCYGSY 328
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
13-359 3.29e-34

Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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: 200473  Cd Length: 447  Bit Score: 136.15  E-value: 3.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNtsnnpsgalfSSGCtnlrkycgGDWQGIINKINdgYLTDMGVTAIWIS--QPvenvfSVMNDAsgs 90
Cdd:cd11334   6 VIYQLDVRTFMDSN----------GDGI--------GDFRGLTEKLD--YLQWLGVTAIWLLpfYP-----SPLRDD--- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       91 asyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPA---------------------SETNPSYME 149
Cdd:cd11334  58 ----GYDIADYYGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQhpwfqaarrdpdspyrdyyvwSDTPPKYKD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      150 NGRLYdNGTLLGGYTND--ANMYFHHnggtTFSSLEdgiyrnlfdlADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAV 227
Cdd:cd11334 134 ARIIF-PDVEKSNWTWDevAGAYYWH----RFYSHQ----------PDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAV 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      228 KHM-------------PFGWQKSLMDEIDNYRPvftfGEWFLSENEVDANN--HYFANESGMSLL-DFRFGQKLRQVLRN 291
Cdd:cd11334 199 PYLieregtncenlpeTHDFLKRLRAFVDRRYP----DAILLAEANQWPEEvrEYFGDGDELHMAfNFPLNPRLFLALAR 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      292 nsdnwygfnqmiQDTASAYDeVLDQ----------VTFIDNHD---------------MDRFMID--------------- 331
Cdd:cd11334 275 ------------EDAFPIID-ALRQtppipegcqwANFLRNHDeltlemltdeerdyvYAAFAPDprmriynrgirrrla 341
                       410       420       430
                ....*....|....*....|....*....|.
1CYG_A      332 ---GGDPRKVDMALAVLLTSRGVPNIYYGTE 359
Cdd:cd11334 342 pmlGGDRRRIELAYSLLFSLPGTPVIYYGDE 372
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
495-576 1.74e-33

IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown.


Pssm-ID: 238338  Cd Length: 81  Bit Score: 124.76  E-value: 1.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      495 PIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYdNFEV 574
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGY-NFEV 79

                ..
1CYG_A      575 LT 576
Cdd:cd00604  80 LT 81
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
581-678 5.88e-33

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 123.56  E-value: 5.88e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      581 SVRFVVNNaTTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQvvySYPTWYIDVSVP--EGKTIEFKFIKKDSQGNVTWES 658
Cdd:cd05467   1 QVRFQVRC-TTQFGQSVYVVGSHPELGNWDPAKALRLNTSN---SYPLWTGEIPLPapEGQVIEYKYVIVDDDGNVQWES 76
                        90       100
                ....*....|....*....|
1CYG_A      659 GSNHVYTTPTNTTGKIIVDW 678
Cdd:cd05467  77 GSNRVLTVPSTSSLIVVDDW 96
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
13-374 2.87e-32

Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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: 200472  Cd Length: 428  Bit Score: 130.27  E-value: 2.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSnnpsgalfssgctnlrkycG-GDWQGIINKIndGYLTDMGVTAIWISqPVenvF-SVMNDasgs 90
Cdd:cd11333   4 VVYQIYPRSFKDSNGD-------------------GiGDLPGIISKL--DYLKDLGVDAIWLS-PI---YpSPQVD---- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       91 asyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P------ASETNPsYM--------ENGRL 153
Cdd:cd11333  55 ---NGYDISDYRAIDPEFGTMEDFDELIKEAHKRGIKIIMDLVVNHTSdehPwfqesrSSRDNP-YRdyyiwrdgKDGKP 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      154 YDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLFDL--ADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDA 226
Cdd:cd11333 131 PNNwRSFFGGsaweYDPETGQYYLH----------------LFAKeqPDLNWENPEVRQEIYDMMRFWLDKGVDGFRLDV 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      227 VKHM----------------PFGWQ------------KSLMDEIDNYRPVFTFGE-WFLSENE----VDANNHYF----- 268
Cdd:cd11333 195 INLIskdpdfpdappgdgdgLSGHKyyangpgvheylQELNREVFSKYDIMTVGEaPGVDPEEalkyVGPDRGELsmvfn 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      269 --------ANESGMSLLDFRFgQKLRQVLrnnsDNWYgfNQMIQDTASAYdevldqvtFIDNHDM----DRFmidgGDPR 336
Cdd:cd11333 275 fehldldyGPGGKWKPKPWDL-EELKKIL----SKWQ--KALQGDGWNAL--------FLENHDQprsvSRF----GNDG 335
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
1CYG_A      337 KVDM----ALA-VLLTSRGVPNIYYGTEQYMTgNGDPNNRKMM 374
Cdd:cd11333 336 EYRVesakMLAtLLLTLRGTPFIYQGEEIGMT-NSRDNARTPM 377
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-363 3.66e-31

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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: 200470  Cd Length: 450  Bit Score: 127.06  E-value: 3.66e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNtsnnpsgalfSSGCtnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPVenvF-SVMNDAsgsa 91
Cdd:cd11331   7 VIYQIYPRSFQDSN----------GDGV--------GDLRGIISRL--DYLSDLGVDAVWLS-PI---YpSPMADF---- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       92 syhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS---P------ASETNPS---YmengrLYDNGTL 159
Cdd:cd11331  59 ---GYDVSDYCGIDPLFGTLEDFDRLVAEAHARGLKVILDFVPNHTSdqhPwflesrSSRDNPKrdwY-----IWRDPAP 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      160 LGGYTNDANMYFhhnGGT--TFSSLEDGIYRNLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMpfGWQ 235
Cdd:cd11331 131 DGGPPNNWRSEF---GGSawTWDERTGQYYLHAFlpEQPDLNWRNPEVRAAMHDVLRFWLDRGVDGFRVDVLWLL--IKD 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      236 KSLMDEIDN--YRPVFTFGEWFL---SENEVDAnnHYFAneSGMSLLDFRFGQK---------LRQVLRnnsdnWYG--- 298
Cdd:cd11331 206 PQFRDNPPNpdWRGGMPPHERLLhiyTADQPET--HEIV--REMRRVVDEFGDRvligeiylpLDRLVA-----YYGagr 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      299 ------FN----------QMIQDTASAYDEVLDQVT----FIDNHDMDRFMIDGGdPRKVDMALAVLLTSRGVPNIYYGT 358
Cdd:cd11331 277 dglhlpFNfhlislpwdaAALARAIEEYEAALPAGAwpnwVLGNHDQPRIASRVG-PAQARVAAMLLLTLRGTPTLYYGD 355

                ....*
1CYG_A      359 EQYMT 363
Cdd:cd11331 356 ELGME 360
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
579-680 4.66e-31

Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99893  Cd Length: 103  Bit Score: 118.86  E-value: 4.66e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      579 QVSVRFVVNNA-TTNLGQNIYIVGNVYELGNW--DTSKAIGPMFNQvvySYPTWYIDVSVPEGKTIEFKFIKKDSQGNVT 655
Cdd:cd05820   2 QIPVIFTVQNTpETAPGEFLYLTGSVPELGNWstSTDQAVGPLLCP---NWPDWFVVASVPAGTYIEFKFLKAPADGTGT 78
                        90       100
                ....*....|....*....|....*
1CYG_A      656 WESGSNHVYTTPTNTTGKIIVDWQN 680
Cdd:cd05820  79 WEGGSNHAYTTPSGGTGTVTVTWQR 103
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
55-404 4.64e-30

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  Cd Length: 366  Bit Score: 122.67  E-value: 4.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       55 INKIND--GYLTDMGVTAIWISqPVenvFSvmndasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDF 132
Cdd:cd11353  29 ILKLEDwiPHLKKLGINAIYFG-PV---FE--------SDSHGYDTRDYYKIDRRLGTNEDFKAVCKKLHENGIKVVLDG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      133 APNHTS---PASETNPSYMENGRlydngtllggYTNdanmYFHhngGTTF---SSLEDGIY----RNLFDLADLNHQNPV 202
Cdd:cd11353  97 VFNHVGrdfFAFKDVQENRENSP----------YKD----WFK---GVNFdgnSPYNDGFSyegwEGHYELVKLNLHNPE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      203 IDRYLKDAVKMWID-MGIDGIRMDAVKHMPFGWQKSLMDEIDNYRPVFtfgeWFLSenEV---DANnhYFANE------- 271
Cdd:cd11353 160 VVDYLFDAVRFWIEeFDIDGLRLDVADCLDFDFLRELRDFCKSLKPDF----WLMG--EVihgDYN--RWANDemldsvt 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      272 ---------SGMSLLD-FRFGQKLRQvlRNNSDNWYGFNQMiqdtasaydevldqVTFIDNHDMDRFMIDGGDPRKVDMA 341
Cdd:cd11353 232 nyecykglySSHNDHNyFEIAHSLNR--QFGLEGIYRGKHL--------------YNFVDNHDVNRIASILKNKEHLPPI 295
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      342 LAVLLTSRGVPNIYYGTEQYMTG----NGDPNNR---KMMSSFNKNTRAYQVIQKLSSLRRNNPALAYGD 404
Cdd:cd11353 296 YALLFTMPGIPSIYYGSEWGIEGvkgnGSDAALRpalDEPELSGENNELTDLIAKLARIRRASPALCYGS 365
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
49-400 2.58e-29

Alpha amylase catalytic domain found in an uncharacterized protein 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; 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 (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: 200488  Cd Length: 390  Bit Score: 120.84  E-value: 2.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       49 GDWQGIINKINdgYLTDMGVTAIWIsQPVENVfsVMNDASGSASYHgYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11350  30 GDFKGVIDKLD--YLQDLGVNAIEL-MPVQEF--PGNDSWGYNPRH-YFA-----LDKAYGTPEDLKRLVDECHQRGIAV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      129 IIDFAPNHtspASETNPSYmengRLYDNGtllGGYTNDANMYFHHNGGTTFSSledgiyrnlfDLADLNHQNPVIDRYLK 208
Cdd:cd11350  99 ILDVVYNH---AEGQSPLA----RLYWDY---WYNPPPADPPWFNVWGPHFYY----------VGYDFNHESPPTRDFVD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      209 DAVKMWID-MGIDGIRMDAVKHMpfgWQK-SLMDEIDNYRP-VFTFGEWFLSENEVDANNHYF-------------ANES 272
Cdd:cd11350 159 DVNRYWLEeYHIDGFRFDLTKGF---TQKpTGGGAWGGYDAaRIDFLKRYADEAKAVDKDFYViaehlpdnpeeteLATY 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      273 GMSLLDFRFGQKLRQVLRNNSDN------WYGFNQMIQDTASAydevldqVTFIDNHDMDRFM------------IDGGD 334
Cdd:cd11350 236 GMSLWGNSNYSFSQAAMGYQGGSllldysGDPYQNGGWSPKNA-------VNYMESHDEERLMyklgaygngnsyLGINL 308
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CYG_A      335 P---RKVDMALAVLLTSRGVPNIY------YGTEQYMTGNGDPNNRKMMSSF---NKNTRAYQVIQKLSSLRRNNPAL 400
Cdd:cd11350 309 EtalKRLKLAAAFLFTAPGPPMIWqggefgYDYSIPEDGRGTTLPKPIRWDYlydPERKRLYELYRKLIKLRREHPAL 386
malS PRK09505
alpha-amylase; Reviewed
14-429 8.90e-29

alpha-amylase; Reviewed


Pssm-ID: 236543  Cd Length: 683  Bit Score: 122.08  E-value: 8.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        14 VYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYCGGDWQGIINKINdgYLTDMGVTAIWISQPVENVFS-VMNDASGSA- 91
Cdd:PRK09505 192 VYFVLTDRFENGDPSNDHSYGRHKDGMQEIGTFHGGDLRGLTEKLD--YLQQLGVNALWISSPLEQIHGwVGGGTKGDFp 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        92 --SYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGT----LLGGYTN 165
Cdd:PRK09505 270 hyAYHGYYTLDWTKLDANMGTEADLRTLVDEAHQRGIRILFDVVMNHTGYATLADMQEFQFGALYLSGDenkkTLGERWS 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       166 D----ANMYFHH------------------------NGGTTFSSLEDGIYRNLFDLADL--NHQNPV------------- 202
Cdd:PRK09505 350 DwqpaAGQNWHSfndyinfsdstawdkwwgkdwirtDIGDYDNPGFDDLTMSLAFLPDIktESTQASglpvfyankpdtr 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       203 ---IDRYLK-DAVKMWI-----DMGIDGIRMDAVKHM-PFGWQKsLMDEIDNyrpvfTFGEW-------------FLSEN 259
Cdd:PRK09505 430 akaIDGYTPrDYLTHWLsqwvrDYGIDGFRVDTAKHVeLPAWQQ-LKQEASA-----ALAEWkkanpdkalddapFWMTG 503
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       260 EVDAN----NHYFANesGM-SLLDFRF-GQKLRQV--LRNNSDNWYGFNQMIQDtasaydevLDQVTFIDNHDMDRFMID 331
Cdd:PRK09505 504 EAWGHgvmkSDYYRH--GFdAMINFDYqEQAAKAVdcLAQMDPTYQQMAEKLQD--------FNVLSYLSSHDTRLFFEG 573
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       332 GGDPRKVDMALAVLLTSRGVPNIYYGTE--QYMTGNGDPNNRKMMSSFN----KNTRAYQVI--QKLSSLRRNNPALAYG 403
Cdd:PRK09505 574 GQSYAKQRRAAELLLLAPGAVQIYYGDEsaRPFGPTGSDPLQGTRSDMNwqevSGKSAALLAhwQKLGQFRARHPAIGAG 653
                        490       500
                 ....*....|....*....|....*..
1CYG_A       404 dtEQRWI-NGDVYVYERQFGKDVVLVA 429
Cdd:PRK09505 654 --KQTTLsLKQYYAFVREHGDDKVMVV 678
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
49-230 2.20e-28

Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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: 200467  Cd Length: 470  Bit Score: 118.87  E-value: 2.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       49 GDWQGIINKIndGYLTDMGVTAIWISQPVEnvfSVMNDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11328  27 GDLKGITEKL--DYFKDIGIDAIWLSPIFK---SPMVDF-------GYDISDFTDIDPIFGTMEDFEELIAEAKKLGLKV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      129 IIDFAPNHTSPASE-------TNPSYME-----NGRLYDNGTLL---------GG----YTNDANMYFHHNggttFSSle 183
Cdd:cd11328  95 ILDFVPNHSSDEHEwfqksvkRDEPYKDyyvwhDGKNNDNGTRVppnnwlsvfGGsawtWNEERQQYYLHQ----FAV-- 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1CYG_A      184 dgiyrnlfDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM 230
Cdd:cd11328 169 --------KQPDLNYRNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHL 207
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-359 6.44e-28

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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: 200469  Cd Length: 472  Bit Score: 117.36  E-value: 6.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNtsnnpsgalfssgctnlrkycG---GDWQGIINKINdgYLTDMGVTAIWISqPVenvF-SVMNDas 88
Cdd:cd11330   7 VIYQIYPRSFLDSN---------------------GdgiGDLPGITEKLD--YIASLGVDAIWLS-PF---FkSPMKD-- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       89 gsasyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP---------ASETNPS---YM-----ENG 151
Cdd:cd11330  58 -----FGYDVSDYCAVDPLFGTLDDFDRLVARAHALGLKVMIDQVLSHTSDqhpwfeesrQSRDNPKadwYVwadpkPDG 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      152 RLYDNG-TLLGG----YTNDANMYFHHNggttFssledgiyrnLFDLADLNHQNP-VIDRYLkDAVKMWIDMGIDGIRMD 225
Cdd:cd11330 133 SPPNNWlSVFGGsawqWDPRRGQYYLHN----F----------LPSQPDLNFHNPeVQDALL-DVARFWLDRGVDGFRLD 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      226 AVK-HM------------------------PFGWQ---------------KSLMDEIDNYRPVFTFGEwFLSENEVDANN 265
Cdd:cd11330 198 AVNfYMhdpalrdnpprppderedgvaptnPYGMQlhihdksqpenlaflERLRALLDEYPGRFLVGE-VSDDDPLEVMA 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      266 HYFANESGM------SLLDFRFGQKlrqVLRNnsdnwygfnqMIQDTASAYDEVLDQVTFiDNHDM----DRFMIDGGDP 335
Cdd:cd11330 277 EYTSGGDRLhmaysfDLLGRPFSAA---VVRD----------ALEAFEAEAPDGWPCWAF-SNHDVpravSRWAGGADDP 342
                       410       420
                ....*....|....*....|....
1CYG_A      336 RKVDMALAVLLTSRGVPNIYYGTE 359
Cdd:cd11330 343 ALARLLLALLLSLRGSVCLYQGEE 366
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
580-677 1.91e-27

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886  Cd Length: 106  Bit Score: 108.51  E-value: 1.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:cd05811   7 VAVTFNER-VTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKESDGSVTWESD 85
                        90
                ....*....|....*...
1CYG_A      660 SNHVYTTPTNTTGKIIVD 677
Cdd:cd05811  86 PNRSYTVPSGCGTTATVD 103
CBM_2 smart01065
Starch binding domain;
580-668 2.52e-27

Starch binding domain;


Pssm-ID: 215006  Cd Length: 88  Bit Score: 107.82  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgPMfNQVVYSYPTWYIDVSVPE-GKTIEFKFIKKDSQGNVTWES 658
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAV-PL-SPDTDGYPLWKGTVSLPPaGTTIEYKYVKVDEDGSVTWES 78
                           90
                   ....*....|
1CYG_A         659 GSNHVYTTPT 668
Cdd:smart01065  79 GPNRRLTVPE 88
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
580-671 6.85e-26

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 103.98  E-value: 6.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      580 VSVRFVVNnATTNLGQNIYIVGNVYELGNWDTSKAIgPMFNQvvySYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESG 659
Cdd:cd05808   1 VAVTFNVT-ATTVWGQNVYVVGNVPELGNWSPANAV-ALSAA---TYPVWSGTVDLPAGTAIEYKYIKKDGSGTVTWESG 75
                        90
                ....*....|..
1CYG_A      660 SNHVYTTPTNTT 671
Cdd:cd05808  76 PNRTATTPASGT 87
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
13-230 8.38e-25

Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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: 200471  Cd Length: 481  Bit Score: 108.13  E-value: 8.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPvenvF--SVMNDasgs 90
Cdd:cd11332   7 VVYQVYPRSFADANGDGI------------------GDLAGIRARL--PYLAALGVDAIWLS-P----FypSPMAD---- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       91 asyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-------------PASETNPSYM-ENGRlYDN 156
Cdd:cd11332  58 ---GGYDVADYRDVDPLFGTLADFDALVAAAHELGLRVIVDIVPNHTSdqhpwfqaalaagPGSPERARYIfRDGR-GPD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      157 GTLLggyTNDANMYFhhnGG-----TTFSSLEDG-IYRNLFDLA--DLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDaVK 228
Cdd:cd11332 134 GELP---PNNWQSVF---GGpawtrVTEPDGTDGqWYLHLFAPEqpDLNWDNPEVRAEFEDVLRFWLDRGVDGFRID-VA 206

                ..
1CYG_A      229 HM 230
Cdd:cd11332 207 HG 208
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
13-230 7.72e-24

Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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: 200494  Cd Length: 456  Bit Score: 105.13  E-value: 7.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKIndGYLTDMGVTAIWISqPVENvfSVMNDAsgsas 92
Cdd:cd11359   7 VIYQIYPRSFKDSNGDGN------------------GDLKGIREKL--DYLKYLGVKTVWLS-PIYK--SPMKDF----- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       93 yhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASE--------TNPsymengrlYDNGTLLGGYT 164
Cdd:cd11359  59 --GYDVSDFTDIDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNHTSDKHEwfqlsrnsTNP--------YTDYYIWADCT 128
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1CYG_A      165 NDANMYFHHN-----GGTTFSSLE--DGIYRNLFDLA--DLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHM 230
Cdd:cd11359 129 ADGPGTPPNNwvsvfGNSAWEYDEkrNQCYLHQFLKEqpDLNFRNPDVQQEMDDVLRFWLDKGVDGFRVDAVKHL 203
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
49-362 1.00e-23

Alpha amylase catalytic domain found in an uncharacterized protein 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; 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 catalytic triad (DED) is not present here. 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: 200486  Cd Length: 429  Bit Score: 104.31  E-value: 1.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       49 GDWQGIINKINdgYLTDMGVTAIWISQPVENVFSvmnDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:cd11348  19 GDLQGIISKLD--YIKSLGCNAIWLNPCFDSPFK---DA-------GYDVRDYYKVAPRYGTNEDLVRLFDEAHKRGIHV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      129 IIDFAPNHTspaSETNPSYMENGRLYDNgtllgGYTND---ANMYFHHNGGTTFSSLE---DGIYR-NLFDLAD-LNH-- 198
Cdd:cd11348  87 LLDLVPGHT---SDEHPWFKESKKAENN-----EYSDRyiwTDSIWSGGPGLPFVGGEaerNGNYIvNFFSCQPaLNYgf 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      199 --------QNPVID-------RYLKDAVKMWIDMGIDGIRMDA----VKHMPFG------WQKsLMDEIDNYRPVFTF-G 252
Cdd:cd11348 159 ahpptepwQQPVDApgpqatrEAMKDIMRFWLDKGADGFRVDMadslVKNDPGNketiklWQE-IRAWLDEEYPEAVLvS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      253 EWFLSENEVDANNH-----YFANESGMSLLdfrfgQKLRQVLRNNSDNWYgFNQ----MIQDTASAYDEVLDQVT---FI 320
Cdd:cd11348 238 EWGNPEQSLKAGFDmdfllHFGGNGYNSLF-----RNLNTDGGHRRDNCY-FDAsgkgDIKPFVDEYLPQYEATKgkgYI 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
1CYG_A      321 D----NHDMDRfMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYM 362
Cdd:cd11348 312 SlptcNHDTPR-LNARLTEEELKLAFAFLLTMPGVPFIYYGDEIGM 356
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
90-405 2.95e-23

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  Cd Length: 357  Bit Score: 102.02  E-value: 2.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       90 SASyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTspaSETNPSYMEngrlydngTLLGGYTNDANM 169
Cdd:cd11354  56 SAS-HGYDTLDHYRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHV---GRSHPAVAQ--------ALEDGPGSEEDR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      170 YFHHNGGTTFSSLEDGIyrnlfDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMP--FgWQKSLMDEIDNYRP 247
Cdd:cd11354 124 WHGHAGGGTPAVFEGHE-----DLVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPpeF-WARVLPRVRERHPD 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      248 VFTFGEwflsenEVDANNHYFANESGM-SLLDFRFGQKLRQVLRNNsdNWYGFNQMIQDTASAYDEVLDQvTFIDNHDMD 326
Cdd:cd11354 198 AWILGE------VIHGDYAGIVAASGMdSVTQYELWKAIWSSIKDR--NFFELDWALGRHNEFLDSFVPQ-TFVGNHDVT 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      327 RFMIDGGdPRKVDMALAVLLTSRGVPNIYYGTEQYMTG------NGDPNNRKMM-----SSFNKNTRAYQVIQKLSSLRR 395
Cdd:cd11354 269 RIASQVG-DDGAALAAAVLFTVPGIPSIYYGDEQGFTGvkeeraGGDDAVRPAFpaspaELAPLGEWIYRLHQDLIGLRR 347
                       330
                ....*....|
1CYG_A      396 NNPALAYGDT 405
Cdd:cd11354 348 RHPWLHRART 357
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
65-355 4.78e-23

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  Cd Length: 352  Bit Score: 101.20  E-value: 4.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       65 DMGVTAIWISqPVEnvFSVMNDASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASetn 144
Cdd:cd11315  24 AAGYTAIQTS-PPQ--KSKEGGNEGGNWWYRYQPTDYRIGNNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHMANEG--- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      145 psymeNGRLYDNGTLLGGYTNDANmYFHHNGGTT-FSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIR 223
Cdd:cd11315  98 -----SAIEDLWYPSADIELFSPE-DFHGNGGISnWNDRWQVTQGRLGGLPDLNTENPAVQQQQKAYLKALVALGVDGFR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      224 MDAVKHMP----FGWQKSLMDEI---DNYRPVFTFGEwFLSENEvDANNHYFANESGMSLLDFRFGQKLRQVLRNNsdNW 296
Cdd:cd11315 172 FDAAKHIElpdePSKASDFWTNIlnnLDKDGLFIYGE-VLQDGG-SRDSDYASYLSLGGVTASAYGFPLRGALKNA--FL 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CYG_A      297 YGFNQMIQDTASAYDEvlDQ-VTFIDNHDM---DRFMIDGGDPRKVDMALAVLLtSR--GVPNIY 355
Cdd:cd11315 248 FGGSLDPASYGQALPS--DRaVTWVESHDTynnDGFESTGLDDEDERLAWAYLA-ARdgGTPLFF 309
trehalose_treC TIGR02403
alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many ...
8-369 6.12e-23

alpha,alpha-phosphotrehalase; Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.


Pssm-ID: 274115  Cd Length: 543  Bit Score: 103.19  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A          8 NFTSDVVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKINdgYLTDMGVTAIWISqPVenVFSVMNDa 87
Cdd:TIGR02403   1 WWQKKVIYQIYPKSFYDSTGDGT------------------GDLRGIIEKLD--YLKKLGVDYIWLN-PF--YVSPQKD- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         88 sgsasyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-------PASETNPSYM-------ENGRL 153
Cdd:TIGR02403  57 ------NGYDVSDYYAINPLFGTMADFEELVSEAKKRNIKIMLDMVFNHTStehewfkKALAGDSPYRdfyiwrdPKGKP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        154 YDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLFDL--ADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDa 226
Cdd:TIGR02403 131 PTNwQSKFGGsaweYFGDTGQYYLH----------------LFDKtqADLNWENPEVREELKDVVNFWRDKGVDGFRLD- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        227 VKHMPFGWQKSLMDEIDNYRPVFTFG---EWFLSEnevdANNHYFANESGMSL---------------------LDFRFG 282
Cdd:TIGR02403 194 VINLISKDQFFEDDEIGDGRRFYTDGprvHEYLQE----MNQEVFGDNDSVTVgemssttiencirysnpenkeLSMVFT 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        283 QKLRQVLRNNSDNW----YGFNQM--IQDTASAYDEVLD--QVTFIDNHDMDRFMIDGGDPRK-----VDMALAVLLTSR 349
Cdd:TIGR02403 270 FHHLKVDYPNGEKWtlakFDFAKLkeIFSTWQTGMQAGGgwNALFWNNHDQPRAVSRFGDDGEyrvesAKMLAAAIHLLR 349
                         410       420
                  ....*....|....*....|
1CYG_A        350 GVPNIYYGTEQYMTGNGDPN 369
Cdd:TIGR02403 350 GTPYIYQGEEIGMTNPKFTN 369
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
51-487 3.66e-22

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518  Cd Length: 479  Bit Score: 99.96  E-value: 3.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        51 WQGIINKINDgyLTDMGVTAIWI---SQPVENVFSVmndasgsasyhGYWARDFKKPNPF---------FGTLSDFQRLV 118
Cdd:PRK09441  21 WNRLAERAPE--LAEAGITAVWLppaYKGTSGGYDV-----------GYGVYDLFDLGEFdqkgtvrtkYGTKEELLNAI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       119 DAAHAKGIKVIIDFAPNHTSPA--SETNPSYM--ENGRLYDNGTLLG--GYTN-----DANMY------FHHNGGTTFSS 181
Cdd:PRK09441  88 DALHENGIKVYADVVLNHKAGAdeKETFRVVEvdPDDRTQIISEPYEieGWTRftfpgRGGKYsdfkwhWYHFSGTDYDE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       182 L--EDGIYRNLFD-------------------LADLNHQNPVIDRYLKDAVKMWID-MGIDGIRMDAVKHMPFGWQKSLM 239
Cdd:PRK09441 168 NpdESGIFKIVGDgkgwddqvddengnfdylmGADIDFRHPEVREELKYWAKWYMEtTGFDGFRLDAVKHIDAWFIKEWI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       240 DEIDNY--RPVFTFGE-WflsENEVDANNHYFAN-ESGMSLLDFRFGQKLRQVLRNNSDnwYGFNQMIQDTASAYDEVLd 315
Cdd:PRK09441 248 EHVREVagKDLFIVGEyW---SHDVDKLQDYLEQvEGKTDLFDVPLHYNFHEASKQGRD--YDMRNIFDGTLVEADPFH- 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       316 QVTFIDNHDMDRfmIDGGDPRKVD----MALAVLLT-SRGVPNI----YYGTEQYMTGNGDPNnrkmmssfnkntrayqV 386
Cdd:PRK09441 322 AVTFVDNHDTQP--GQALESPVEPwfkpLAYALILLrEEGYPCVfygdYYGASGYYIDMPFKE----------------K 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       387 IQKLSSLRRNnpaLAYGDTEQRWINGDVYVYERQ---FGKDVVLVAVNRSSSSNYSITGlfTALPAGTYTDQLGGLldGN 463
Cdd:PRK09441 384 LDKLLLARKN---FAYGEQTDYFDHPNCIGWTRSgdeENPGLAVVISNGDAGEKTMEVG--ENYAGKTWRDYTGNR--QE 456
                        490       500
                 ....*....|....*....|....
1CYG_A       464 TIQVGSNGSVNaFDLGPGEVGVWA 487
Cdd:PRK09441 457 TVTIDEDGWGT-FPVNGGSVSVWV 479
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
580-671 4.88e-22

Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 14, which hydrolyzes the alpha-1,4-glucosidic bonds of starch, yielding beta-maltose from the nonreducing end of the substrate. Beta-amylase is found in both plants and microorganisms, however the plant members lack a C-terminal CBM20 domain and are not included in this group. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99884  Cd Length: 99  Bit Score: 93.08  E-value: 4.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSkaIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQG-NVTWES 658
Cdd:cd05809   3 VPQTFVVKNVPTTIGETVYITGSRAELGNWDTK--QYPIQLYYNSHSNDWRGTVHLPAGRNIEFKAIKKSKDGtNKSWQG 80
                        90
                ....*....|...
1CYG_A      659 GSNHVYTTPTNTT 671
Cdd:cd05809  81 GQQSWYPVPLGTT 93
treS_nterm TIGR02456
trehalose synthase; Trehalose synthase interconverts maltose and alpha, alpha-trehalose by ...
9-433 1.31e-20

trehalose synthase; Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (). [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274140  Cd Length: 539  Bit Score: 95.97  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A          9 FTSDVVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKINdgYLTDMGVTAIWISQPVEnvfSVMNDAs 88
Cdd:TIGR02456   3 YKDAVFYEVHVRSFFDSNGDGI------------------GDFPGLTSKLD--YLKWLGVDALWLLPFFQ---SPLRDD- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         89 gsasyhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS------PASETNPS--------YMENGRLY 154
Cdd:TIGR02456  59 ------GYDVSDYRAILPEFGTIDDFKDFVDEAHARGMRVIIDLVLNHTSdqhpwfQEARSNPDgpyrdfyvWSDTDEKY 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        155 DNGTLLGGYTNDANMYFHHNGGTTFssledgIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVkhmPFGW 234
Cdd:TIGR02456 133 KDTRIIFVDTEKSNWTFDPVAKQYY------WHRFFSHQPDLNYDNPAVHDAVHDVMRFWLDLGVDGFRLDAV---PYLY 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        235 Q----------------KSLMDEIDNYRPvftfGEWFLSE-----NEVDAnnhYFANESGMSL-LDFRFGQKLRQVLRNN 292
Cdd:TIGR02456 204 EregtscenlpetheflKRLRKMVDREYP----GRMLLAEanqwpEEVVA---YFGDEGDPEChMAFNFPVMPRIFMALR 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        293 SDNWYGFNQMIQDTaSAYDEVLDQVTFIDNHD---------------------MDRFMID-----------GGDPRKVDM 340
Cdd:TIGR02456 277 REDRSPIIDILKET-PDIPDSCQWCIFLRNHDeltlemvtdeerdfmyaayapDPRMRINlgirrrlapllDNDRRRIEL 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        341 ALAVLLTSRGVPNIYYGTEQYMTGN---GDPNNRK--MMSSFNKN---TRA----------------YQVI--------- 387
Cdd:TIGR02456 356 LTALLLSLPGSPILYYGDEIGMGDNiwlGDRNGVRtpMQWSPDRNagfSSAdpgqlflppvqdpvygYQQVnveaqlrdp 435
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
1CYG_A        388 -------QKLSSLRRNNPALAYGD-TEQRWINGDVYVYERQFGKDVVLVAVNRS 433
Cdd:TIGR02456 436 ssllhwtRRVLHVRKAHPAFGRGSlTFLPTGNRRVLAFLREYEGERVLCVFNFS 489
PRK14510 PRK14510
putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional
42-404 6.97e-20

putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional


Pssm-ID: 237739  Cd Length: 1221  Bit Score: 94.57  E-value: 6.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         42 NLRkycgGDWQGIINKINDGYLTDMGVTAIWISQPVENVFSVMNDASGSASYHGYWARDFKKPNPFFGTLS--DFQRLVD 119
Cdd:PRK14510  179 NLR----GTFAKLAAPEAISYLKKLGVSIVELNPIFASVDEHHLPQLGLSNYWGYNTVAFLAPDPRLAPGGeeEFAQAIK 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        120 AAHAKGIKVIIDFAPNHTSPASETNPSymengrlydngtlLGGYTNDANMYFHHNGGTTFSSLEDGIYRNLFDLadlnHQ 199
Cdd:PRK14510  255 EAQSAGIAVILDVVFNHTGESNHYGPT-------------LSAYGSDNSPYYRLEPGNPKEYENWWGCGNLPNL----ER 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        200 NPVIdRYLKDAVKMWIDMGIDGIR---------------------MDAVKHMPFGWQKSLMDE----------IDNYRPv 248
Cdd:PRK14510  318 PFIL-RLPMDVLRSWAKRGVDGFRldladelarepdgfidefrqfLKAMDQDPVLRRLKMIAEvwddglggyqYGKFPQ- 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        249 fTFGEWflSENEVDANNHYFANESGMSlldfrfGQKLRQVLrNNSDNW-----YGFNQMIQDTASAYDEVLDQVTFIDNH 323
Cdd:PRK14510  396 -YWGEW--NDPLRDIMRRFWLGDIGMA------GELATRLA-GSADIFphrrrNFSRSINFITAHDGFTLLDLVSFNHKH 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        324 DMDRFM--IDGGDP--------------------RKVDMA--LAVLLTSRGVPNIYYGTEQYMTGNG------DPNNRKM 373
Cdd:PRK14510  466 NEANGEdnRDGTPDnqswncgvegytldaairslRRRRLRllLLTLMSFPGVPMLYYGDEAGRSQNGnnngyaQDNNRGT 545
                         410       420       430
                  ....*....|....*....|....*....|.
1CYG_A        374 MSSFNKNTRAYQVIQKLSSLRRNNPALAYGD 404
Cdd:PRK14510  546 YPWGNEDEELLSFFRRLIKLRREYGVLRQGE 576
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
580-670 2.44e-19

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 85.15  E-value: 2.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      580 VSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAI--GPMfnqvvySYPTWYIDVSVPEGKTIEFKFIKKDSQG---NV 654
Cdd:cd05810   1 VSVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAVklDPT------AYPTWSGSISLPASTNVEWKCLKRNETNptaGV 74
                        90
                ....*....|....*.
1CYG_A      655 TWESGSNHVYTTPTNT 670
Cdd:cd05810  75 QWQGGGNNQLTTGNST 90
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
13-227 1.96e-17

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849  Cd Length: 551  Bit Score: 85.96  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        13 VVYQIVVDRFVDGNTSNNpsgalfssgctnlrkycgGDWQGIINKINdgYLTDMGVTAIW-----ISQPVENVFSVMNda 87
Cdd:PRK10933  12 VIYQIYPKSFQDTTGSGT------------------GDLRGVTQRLD--YLQKLGVDAIWltpfyVSPQVDNGYDVAN-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        88 sgsasyhgYWARDfkkpnPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTS-----------PASETNPSYM----ENGR 152
Cdd:PRK10933  70 --------YTAID-----PTYGTLDDFDELVAQAKSRGIRIILDMVFNHTStqhawfrealnKESPYRQFYIwrdgEPET 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       153 LYDN-GTLLGG----YTNDANMYFHHnggttfssledgiyrnLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMD 225
Cdd:PRK10933 137 PPNNwRSKFGGsawrWHAESEQYYLH----------------LFapEQADLNWENPAVRAELKKVCEFWADRGVDGLRLD 200

                 ..
1CYG_A       226 AV 227
Cdd:PRK10933 201 VV 202
AmyAc_GTHase cd11325
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ...
48-400 2.41e-17

Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase); Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase


Pssm-ID: 200464  Cd Length: 436  Bit Score: 84.91  E-value: 2.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       48 GGDWQGIINKIndGYLTDMGVTAIWIsQPVenvfsvmNDASGSASYhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIK 127
Cdd:cd11325  51 EGTFDAAIERL--DYLADLGVTAIEL-MPV-------AEFPGERNW-GYDGVLPFAPESSYGGPDDLKRLVDAAHRRGLA 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      128 VIIDFAPNHTSPasetnpsymengrlydNGTLLGGYTNDanmYFHHNGGTTFSsleDGIyrNlFDLADlnhqNPViDRYL 207
Cdd:cd11325 120 VILDVVYNHFGP----------------DGNYLWQFAGP---YFTDDYSTPWG---DAI--N-FDGPG----DEV-RQFF 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      208 KDAVKMWI-DMGIDGIRMDAVKHMPFGWQKSLMDEI-------DNYRPVFTFGewflsenEVDANNH-----YFANESGM 274
Cdd:cd11325 170 IDNALYWLrEYHVDGLRLDAVHAIRDDSGWHFLQELarevraaAAGRPAHLIA-------EDDRNDPrlvrpPELGGAGF 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      275 SLL---DFRfgQKLRQVLRNNSDNWYGFNQMIQDTASAYDEV-LDQ-----------------------VTFIDNHD--- 324
Cdd:cd11325 243 DAQwndDFH--HALHVALTGEREGYYADFGPAEDLARALAEGfVYQgqyspfrgrrhgrpsadlpptrfVVFLQNHDqvg 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      325 ----MDRfMIDGGDPRKVDMALAVLLTSRGVPNIYYGTE-------QYMTGNGDPNNRKMMSSFNKNTRAYQVIQKLSSL 393
Cdd:cd11325 321 nraaGER-LSSLAAPARLRLAAALLLLSPGIPMLFMGEEfgedtpfLFFTDHDDPELAEAVREGRRREFAAGWDRDLIPD 399

                ....*..
1CYG_A      394 RRNNPAL 400
Cdd:cd11325 400 PQAPETF 406
Aamy_C smart00632
Aamy_C domain;
406-490 3.51e-17

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 78.82  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         406 EQRWINGD-VYVYERqfgKDVVLVAVNRSSSsnYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGsVNAFDLGPGE-V 483
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRSDS--DLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPAGGaV 74

                   ....*..
1CYG_A         484 GVWAYSA 490
Cdd:smart00632  75 AIHVDAK 81
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
48-356 8.13e-16

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  Cd Length: 302  Bit Score: 78.42  E-value: 8.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       48 GGDWQGIIN-KINDgyLTDMGVTAIWISQPVEnvfsvmndaSGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGI 126
Cdd:cd11314  13 DGTWWNHLEsKAPE--LAAAGFTAIWLPPPSK---------SVSGSSMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      127 KVIIDFAPNHtspasetnpsymENGrlYDNGTLLGGYTN-DanmyfHHNggttfssleDGIYRNLFDLAdlnhqnpvidR 205
Cdd:cd11314  82 KVIADIVINH------------RSG--PDTGEDFGGAPDlD-----HTN---------PEVQNDLKAWL----------N 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      206 YLKDavkmwiDMGIDGIRMDAVKHMPFGWQKSLMDEIDNYrpvFTFGEWFLSENEVDANNHY-----FANESGM--SLLD 278
Cdd:cd11314 124 WLKN------DIGFDGWRFDFVKGYAPSYVKEYNEATSPS---FSVGEYWDGLSYENQDAHRqrlvdWIDATGGgsAAFD 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      279 FRFGQKLRQVLrnNSDNWYGFNQMiQDTASAYDEVLDQ--VTFIDNHDMDRfmIDGGDP---RKVDMALAVLLTSRGVPN 353
Cdd:cd11314 195 FTTKYILQEAV--NNNEYWRLRDG-QGKPPGLIGWWPQkaVTFVDNHDTGS--TQGHWPfptDNVLQGYAYILTHPGTPC 269

                ...
1CYG_A      354 IYY 356
Cdd:cd11314 270 VFW 272
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
49-230 8.68e-16

1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 223373  Cd Length: 628  Bit Score: 80.82  E-value: 8.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       49 GDWQGIINKINdgYLTDMGVTAIWIsQPVENVfsvmndaSGSASYhGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKV 128
Cdd:COG0296 162 GYFELAIELLP--YLKELGITHIEL-MPVAEH-------PGDRSW-GYQGTGYYAPTSRYGTPEDFKALVDAAHQAGIGV 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      129 IIDFAPNHTSPASETNPSYmengrlydNGTLLGGYTnDANMYFHHNGGTTfssledgiyrnLFDladlNHQNPViDRYLK 208
Cdd:COG0296 231 ILDWVPNHFPPDGNYLARF--------DGTFLYEHE-DPRRGEHTDWGTA-----------IFN----YGRNEV-RNFLL 285
                       170       180
                ....*....|....*....|...
1CYG_A      209 DAVKMWID-MGIDGIRMDAVKHM 230
Cdd:COG0296 286 ANALYWLEeYHIDGLRVDAVASM 308
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
62-357 1.48e-15

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  Cd Length: 391  Bit Score: 79.10  E-value: 1.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAIWISqPvenvfsvMNDASGSASYHGYWARDF--------------KkpnpfFGTLSDFQRLVDAAHAKGIK 127
Cdd:cd11318  28 ELAELGITAVWLP-P-------AYKGASGTEDVGYDVYDLydlgefdqkgtvrtK-----YGTKEELLEAIKALHENGIQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      128 VIIDFAPNH--------TSPASETNPSYmENGRLYDNGTLLG--GYT--NDANMY------FHHNGGTTF--SSLEDGIY 187
Cdd:cd11318  95 VYADAVLNHkagadeteTVKAVEVDPND-RNKEISEPYEIEAwtKFTfpGRGGKYsdfkwnWQHFSGVDYdqKTKKKGIF 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      188 RNLFDL-------------------ADLNHQNPVIDRYLKDAVKmWI--DMGIDGIRMDAVKHMPFGWQKSLMDEIDNY- 245
Cdd:cd11318 174 KINFEGkgwdedvddengnydylmgADIDYSNPEVREELKRWGK-WYinTTGLDGFRLDAVKHISASFIKDWIDHLRREt 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      246 -RPVFTFGEWFlsENEVDANNHYFANESG-MSLLDFrfgqKLRQVLRNNSDNWYGFN--QMIQDTASAYDEVlDQVTFID 321
Cdd:cd11318 253 gKDLFAVGEYW--SGDLEALEDYLDATDGkMSLFDV----PLHYNFHEASKSGGNYDlrKIFDGTLVQSRPD-KAVTFVD 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
1CYG_A      322 NHD------MDRFMIdggDPRKVdMALAV-LLTSRGVPNIYYG 357
Cdd:cd11318 326 NHDtqpgqsLESWVE---PWFKP-LAYALiLLRKDGYPCVFYG 364
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
108-378 2.09e-15

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  Cd Length: 329  Bit Score: 77.60  E-value: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      108 FGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpaseTNPSYMENGRLYDngtllggytndanmyfhhnggttfssledgiy 187
Cdd:cd11317  62 SGTEAEFRDMVNRCNAAGVRVYVDAVINHMA----GDANEVRNCELVG-------------------------------- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      188 rnlfdLADLNHQNP-VIDR---YLKDAvkmwIDMGIDGIRMDAVKHMP-------FGWQKSLMDEIDNYRPvFTFGEWFL 256
Cdd:cd11317 106 -----LADLNTESDyVRDKiadYLNDL----ISLGVAGFRIDAAKHMWpedlaaiLARLKDLNGGPLGSRP-YIYQEVID 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      257 SENEVDANNHYFANesGMsLLDFRFGQKLRQVLRNNSDNWYGFNqmiQDTASAYDEVLDQVTFIDNHDMDRfmiDGG--- 333
Cdd:cd11317 176 GGGEAIQPSEYTGN--GD-VTEFRYARGLSNAFRGKIKLLLLKN---FGEGWGLLPSERAVVFVDNHDNQR---GHGggg 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
1CYG_A      334 ------DPRKVDMALAVLLTSRgvpniyYGTeqymtgngdpnnRKMMSSFN 378
Cdd:cd11317 247 dmltykDGRRYKLANAFMLAWP------YGT------------PRVMSSYY 279
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
581-678 5.45e-14

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 70.05  E-value: 5.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      581 SVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIgpmfnQVVY-SYPTWYIDVSVPEGKT-IEFKFIKKDS-QGNVTWE 657
Cdd:cd05816   1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKAL-----KLSDvGFPIWEADIDISKDSFpFEYKYIIANKdSGVVSWE 75
                        90       100
                ....*....|....*....|....
1CYG_A      658 SGSNHVYTTPTNTTGKIIV---DW 678
Cdd:cd05816  76 NGPNRELSAPSLKGESSTLivsDG 99
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
13-359 6.54e-14

Alpha amylase catalytic domain found in an uncharacterized protein 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; 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: 200487  Cd Length: 456  Bit Score: 74.25  E-value: 6.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       13 VVYQIVVDRFVDGNTSNNPSGALFSSGCtnlrkycggdwqGIINKIND---GYLTDMGVTAIW----ISQPVENVFSVMN 85
Cdd:cd11349   2 IIYQLLPRLFGNKNTTNIPNGTIEENGV------------GKFNDFDDtalKEIKSLGFTHVWytgvIRHATQTDYSAYG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       86 DAS----------GSAsyhgYWARDFKKPNPFFGT-----LSDFQRLVDAAHAKGIKVIIDFAPNHTSPA--SETNPSYM 148
Cdd:cd11349  70 IPPddpdivkgraGSP----YAIKDYYDVDPDLATdptnrMEEFEALVERTHAAGLKVIIDFVPNHVARQyhSDAKPEGV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      149 ENGRLYDNGTLlgGYTNDANMY------FHHNGGTTFSSLEDGIYR---------NLFDLA----------DLN------ 197
Cdd:cd11349 146 KDFGANDDTSK--AFDPSNNFYylpgepFVLPFSLNGSPATDGPYHespakatgnDCFSAApsindwyetvKLNygvdyd 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      198 -----HQNPVIDRYLK--DAVKMWIDMGIDGIRMDAVkHM---PFgWQKsLMDEIDNYRPVFTfgewFLSENEVDANNHY 267
Cdd:cd11349 224 gggsfHFDPIPDTWIKmlDILLFWAAKGVDGFRCDMA-EMvpvEF-WHW-AIPEIKARYPELI----FIAEIYNPGLYRD 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      268 FANESGMSLLDFRFG--QKLRQVLRNNSDNwYGFNQMIQDTASAYDEVLDqvtFIDNHDMDRFMID--GGDPRKVDMALA 343
Cdd:cd11349 297 YLDEGGFDYLYDKVGlyDTLRAVICGGGSA-SEITVWWQESDDIADHMLY---FLENHDEQRIASPffAGNAEKALPAMV 372
                       410
                ....*....|....*..
1CYG_A      344 VLLT-SRGVPNIYYGTE 359
Cdd:cd11349 373 VSATlSTGPFMLYFGQE 389
trehalose_TreZ TIGR02402
malto-oligosyltrehalose trehalohydrolase; Members of this family are the trehalose ...
49-372 1.21e-12

malto-oligosyltrehalose trehalohydrolase; Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274114  Cd Length: 544  Bit Score: 70.44  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         49 GDWQGIINKIndGYLTDMGVTAIWIsQPVenvfsvmNDASGSasyHGyWARD---FKKPNPFFGTLSDFQRLVDAAHAKG 125
Cdd:TIGR02402 108 GTFDAAIEKL--PYLADLGITAIEL-MPV-------AQFPGT---RG-WGYDgvlPYAPHEAYGGPDDLKALVDAAHGLG 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        126 IKVIIDFAPNHTSPASETNPSYmengrlydngtllGGYTNDAnmyfHHNG-GTTFSsledgiyrnlFDLADLNHqnpvID 204
Cdd:TIGR02402 174 LGVLLDVVYNHFGPEGNYLPRF-------------APYFTDR----YSTPwGAAIN----------FDGPGSDE----VR 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        205 RYLKDAVKMWI-DMGIDGIRMDAVKHM----PFGWQKSLMDEIDNY----RPVFtfgewFLSENevDANNHYFAN--ESG 273
Cdd:TIGR02402 223 RYIIDNALYWLrEYHFDGLRLDAVHAIadtsAKHFLEELARAVRELaadlRPVH-----LIAES--DLNDPSLLTprADG 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        274 MSLLDFR----FGQKLRQVLRNNSDNWY-GFNQMIQDTASAYDEVL-------------------DQ-----VTFIDNHD 324
Cdd:TIGR02402 296 GYGLDAQwnddFHHALHVLLTGERQGYYaDFADPLAALAKALAEGFvydgeyspfrgrphgrpsgDLpphrfVVFIQNHD 375
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1CYG_A        325 M-------DRfMIDGGDPRKVDMALAVLLTSRGVPNIYYGTE-------QYMTGNGDPNNRK 372
Cdd:TIGR02402 376 QvgnraqgER-LSQLLSPGSLKLAAALTLLSPYIPLLFMGEEygattpfQFFTDHPDPELAE 436
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
48-236 2.80e-11

Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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: 200463  Cd Length: 536  Bit Score: 66.05  E-value: 2.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       48 GGDWQGIINKINdgYLTDMGVTaiwisqpvenVFSVM---------NDAsgsasyhGYWARDFKKPNPFFGTLSDFQRLV 118
Cdd:cd11324  82 AGDLKGLAEKIP--YLKELGVT----------YLHLMpllkppegdNDG-------GYAVSDYREVDPRLGTMEDLRALA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      119 DAAHAKGIKVIIDFAPNHTS-------PASETNPSYMENGRLYDNGTLL----------------GGYTNDANMyfhhnG 175
Cdd:cd11324 143 AELRERGISLVLDFVLNHTAdehewaqKARAGDPEYQDYYYMFPDRTLPdayertlpevfpdtapGNFTWDEEM-----G 217
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1CYG_A      176 G---TTFSSLEdgiyrnlfdlADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVkhmPFGWQK 236
Cdd:cd11324 218 KwvwTTFNPFQ----------WDLNYANPAVFNEMLDEMLFLANQGVDVLRLDAV---AFIWKR 268
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
62-230 1.89e-10

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  Cd Length: 402  Bit Score: 63.31  E-value: 1.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAIWISQPVENVFSvmndasGSASYH--GYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP 139
Cdd:cd11322  67 YVKEMGYTHVELMPVMEHPFD------GSWGYQvtGYFA-----PTSRYGTPDDFKYFVDACHQAGIGVILDWVPGHFPK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      140 AsetnpsymENGrLYD-NGTLLGGYTnDANMYFHHNGGTtfssledgiyrNLFDLADlnhqnPVIDRYLKDAVKMWID-M 217
Cdd:cd11322 136 D--------DHG-LARfDGTPLYEYP-DPRKGEHPDWGT-----------LNFDYGR-----NEVRSFLISNALYWLEeY 189
                       170
                ....*....|...
1CYG_A      218 GIDGIRMDAVKHM 230
Cdd:cd11322 190 HIDGLRVDAVSSM 202
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
15-132 4.42e-10

Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase); Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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: 200462  Cd Length: 569  Bit Score: 62.31  E-value: 4.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       15 YQIVVDRFVDGNTSNNP-SGALFSSGC--TNLRKycGGDWQGIINKINdgYLTDMGVTAI------WISQPvenvfsvmn 85
Cdd:cd11323  59 YTIFLDRFVNGDPTNDDaNGTVFEQDIyeTQLRH--GGDIVGLVDSLD--YLQGMGIKGIyiagtpFINMP--------- 125
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1CYG_A       86 dasgsASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDF 132
Cdd:cd11323 126 -----WGADGYSPLDFTLLDHHFGTIADWRAAIDEIHRRGMYVVLDN 167
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
591-666 5.84e-10

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 58.25  E-value: 5.84e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CYG_A      591 TNLGQNIYIVGNVYELGNWDTSKAIGPMFNQvvysYPTWYIDVSVPEGKTIEFKFI--KKDSQGNVTWESGSNHVYTT 666
Cdd:cd05817  10 TQFGEAVYISGNCNQLGNWNPSKAKRMQWNE----GDLWTVDVGIPESVYIEYKYFvsNYDDPNTVLWESGPNRVLRT 83
PRK14706 PRK14706
glycogen branching enzyme; Provisional
62-230 7.14e-10

glycogen branching enzyme; Provisional


Pssm-ID: 237795  Cd Length: 639  Bit Score: 61.92  E-value: 7.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        62 YLTDMGVTAIWISQPVENVFsvmnDASGSASYHGYWArdfkkPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTsPAS 141
Cdd:PRK14706 176 YVTYMGYTHVELLGVMEHPF----DGSWGYQVTGYYA-----PTSRLGTPEDFKYLVNHLHGLGIGVILDWVPGHF-PTD 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       142 ETNPSYMENGRLYDNGTLLGGYTNDANMYfhhnggttfssledgiyrnLFDLAdlnhQNPVIDRYLKDAVKMWIDMGIDG 221
Cdd:PRK14706 246 ESGLAHFDGGPLYEYADPRKGYHYDWNTY-------------------IFDYG----RNEVVMFLIGSALKWLQDFHVDG 302

                 ....*....
1CYG_A       222 IRMDAVKHM 230
Cdd:PRK14706 303 LRVDAVASM 311
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
105-242 9.32e-10

Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. 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: 200468  Cd Length: 477  Bit Score: 61.24  E-value: 9.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      105 NPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSP-------ASETNPSYmenGRLYDNGTLLGGYTndANMYFHHNGGT 177
Cdd:cd11329 108 NNSYGVESDLKELVKTAKQKDIKVILDLTPNHSSKqhplfkdSVLKEPPY---RSAFVWADGKGHTP--PNNWLSVTGGS 182
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CYG_A      178 TFSSLED-GIYRNLF--DLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHmpFGWQKSLMDEI 242
Cdd:cd11329 183 AWKWVEDrQYYLHQFgpDQPDLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY--LLEDPNLKDEE 248
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
62-407 1.07e-09

pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.


Pssm-ID: 273975  Cd Length: 605  Bit Score: 61.18  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         62 YLTDMGVTAIWIsQPVeNVFSVMNDASGSASYH-GYWARDFKKPNPFFGT--------LSDFQRLVDAAHAKGIKVIIDF 132
Cdd:TIGR02104 172 YLKELGVTHVQL-LPV-FDFAGVDEEDPNNAYNwGYDPLNYNVPEGSYSTnpydpatrIRELKQMIQALHENGIRVIMDV 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        133 APNHT-----SPASETNPSYmengrlydngtllggytndanmYFHHNggttfsslEDGIYRNLFDLA-DLNHQNPVIDRY 206
Cdd:TIGR02104 250 VYNHTysreeSPFEKTVPGY----------------------YYRYN--------EDGTLSNGTGVGnDTASEREMMRKF 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        207 LKDAVKMWI-DMGIDGIRMDA-----VKHMpfgwqKSLMDEIDNYRP-VFTFGE-WFLS---ENEVDANNhyfANESGMS 275
Cdd:TIGR02104 300 IVDSVLYWVkEYNIDGFRFDLmgihdIETM-----NEIRKALNKIDPnILLYGEgWDLGtplPPEQKATK---ANAYQMP 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        276 LLDFrFGQKLRQVLRNN----------SDNWYGFNQMI----------QDTASAYD--EVLDQVTFIDNHDM-DRFMIDG 332
Cdd:TIGR02104 372 GIAF-FNDEFRDALKGSvfhlkkkgfvSGNPGTEEIVKkgilgsieldAVKPSALDpsQSINYVECHDNHTLwDKLSLAN 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        333 GD------PRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFN------KNTRAYQV--IQKLSSLRRNNP 398
Cdd:TIGR02104 451 PDeteeqlKKRQKLATAILLLSQGIPFLHAGQEFMRTKQGDENSYNSPDSINqldwdrKATFKDDVnyIKGLIALRKAHP 530

                  ....*....
1CYG_A        399 ALAYGDTEQ 407
Cdd:TIGR02104 531 AFRLSSAED 539
PRK14511 PRK14511
maltooligosyl trehalose synthase; Provisional
61-152 2.56e-09

maltooligosyl trehalose synthase; Provisional


Pssm-ID: 237740  Cd Length: 879  Bit Score: 60.38  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        61 GYLTDMGVTAIWISqpvenvfSVMNDASGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPA 140
Cdd:PRK14511  27 PYFADLGVSHLYLS-------PILAARPGST--HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVG 97
                         90
                 ....*....|....*
1CYG_A       141 SETNP---SYMENGR 152
Cdd:PRK14511  98 GPDNPwwwDVLEWGR 112
trehalose_TreY TIGR02401
malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan ...
62-152 2.69e-09

malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, is the TreY enzyme of the TreYZ pathway of trehalose biosynthesis, an alternative to the OtsAB pathway. Trehalose may be incorporated into more complex compounds but is best known as compatible solute. It is one of the most effective osmoprotectants, and unlike the various betaines does not require nitrogen for its synthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274113  Cd Length: 825  Bit Score: 60.11  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         62 YLTDMGVTAIWISqPVEnvfsvmndASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:TIGR02401  24 YLKSLGVSHLYLS-PIL--------TAVPGSTHGYDVVDHSEINPELGGEEGLRRLSEAARARGLGLIVDIVPNHMAVHL 94
                          90
                  ....*....|....
1CYG_A        142 ETNPSYM---ENGR 152
Cdd:TIGR02401  95 EQNPWWWdvlKNGP 108
TreY COG3280
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];
62-152 1.04e-08

Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];


Pssm-ID: 225819  Cd Length: 889  Bit Score: 58.25  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAIWISqPVenvFSVMndaSGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:COG3280  27 YLADLGISHLYLS-PI---FTAR---PGST--HGYDVVDPTEINPELGGEEGLERLVAALKSRGLGLIVDIVPNHMAVGG 97
                        90
                ....*....|....
1CYG_A      142 ETNPSYM---ENGR 152
Cdd:COG3280  98 HENPWWWdvlENGR 111
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
62-152 1.08e-08

Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. 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: 200475  Cd Length: 660  Bit Score: 58.27  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAIWISqPVenvfsvMNDASGSAsyHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPAS 141
Cdd:cd11336  22 YLADLGISHLYAS-PI------LTARPGST--HGYDVVDHTRINPELGGEEGLRRLAAALRAHGMGLILDIVPNHMAVSG 92
                        90
                ....*....|....
1CYG_A      142 ETNPSYM---ENGR 152
Cdd:cd11336  93 AENPWWWdvlENGP 106
glgX_debranch TIGR02100
glycogen debranching enzyme GlgX; This family consists of the GlgX protein from the E. coli ...
42-225 1.25e-08

glycogen debranching enzyme GlgX; This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 131155  Cd Length: 688  Bit Score: 58.13  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A         42 NLRkycgGDWQGIINKINDGYLTDMGVTAI-------WISQPvenvFSVmndASGSASYHGYWARDFKKPNPFF---GTL 111
Cdd:TIGR02100 176 ELR----GTYAGLAHPAMIDYLKKLGVTAVellpvhaFIDDR----HLL---EKGLRNYWGYNTLGFFAPEPRYlasGQV 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        112 SDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGrlYDNGTLLGGYTNDANMYFHHNG-GTTfssledgiyrnl 190
Cdd:TIGR02100 245 AEFKTMVRALHDAGIEVILDVVYNHTAEGNELGPTLSFRG--IDNASYYRLQPDDKRYYINDTGtGNT------------ 310
                         170       180       190
                  ....*....|....*....|....*....|....*.
1CYG_A        191 fdladLNHQNPVIDRYLKDAVKMWI-DMGIDGIRMD 225
Cdd:TIGR02100 311 -----LNLSHPRVLQMVMDSLRYWVtEMHVDGFRFD 341
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
495-576 3.86e-08

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050  Cd Length: 89  Bit Score: 52.46  E-value: 3.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      495 PIIGHVGPMMGQV--GHQVTIDGEGFGTN-TGTVKFGT-TAANVVSWSNNQIVVAVP---NVSPGKYNITVQSSSGQTSA 567
Cdd:cd00102   1 PVITSISPSSGPVsgGTEVTITGSNFGSGsNLRVTFGGgVPCSVLSVSSTAIVCTTPpyaNPGPGPVEVTVDRGNGGITS 80

                ....*....
1CYG_A      568 AYDNFEVLT 576
Cdd:cd00102  81 SPLTFTYVP 89
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
495-573 4.14e-08

IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members.


Pssm-ID: 307788  Cd Length: 85  Bit Score: 52.47  E-value: 4.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        495 PIIGHVGPMMGQV--GHQVTIDGEGFGTNTG--TVKFGTTAANVV-SWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAY 569
Cdd:pfam01833   1 PVITSISPSSGPAsgGTTITITGSNFGTDSSdtKVTIGGTPCTVIaSVSSTTIVCTTPPGTSGLVNVSVTVGGGGLSSSN 80

                  ....
1CYG_A        570 DNFE 573
Cdd:pfam01833  81 LTFT 84
PLN02784 PLN02784
alpha-amylase
63-356 7.99e-08

alpha-amylase


Pssm-ID: 215419  Cd Length: 894  Bit Score: 55.40  E-value: 7.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A        63 LTDMGVTAIWISQPVENVfsvmndasgsaSYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSpase 142
Cdd:PLN02784 530 LSSLGFTVVWLPPPTESV-----------SPEGYMPKDLYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRC---- 594
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       143 tnpSYMENgrlyDNGT--LLGGYTN-DA------NMYFHHNGGTTfssleDGiyrnlfdlaDLNHQNPVIDR---YLKDA 210
Cdd:PLN02784 595 ---AHFQN----QNGVwnIFGGRLNwDDravvadDPHFQGRGNKS-----SG---------DNFHAAPNIDHsqdFVRKD 653
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       211 VKMWI-----DMGIDGIRMDAVKHMpfgWQKSLMDEIDNYRPVFTFGEWF--LSEN--EVDANN--HY-----FANESGM 274
Cdd:PLN02784 654 LKEWLcwmrkEVGYDGWRLDFVRGF---WGGYVKDYMEASEPYFAVGEYWdsLSYTygEMDYNQdaHRqrivdWINATNG 730
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       275 SLLDFRFGQK--LRQVLrNNSDNWygfnqMIQDTASAYDEVLD-----QVTFIDNHDMD------RFmidggdPRKVDM- 340
Cdd:PLN02784 731 TAGAFDVTTKgiLHSAL-ERCEYW-----RLSDQKGKPPGVVGwwpsrAVTFIENHDTGstqghwRF------PEGKEMq 798
                        330
                 ....*....|....*.
1CYG_A       341 ALAVLLTSRGVPNIYY 356
Cdd:PLN02784 799 GYAYILTHPGTPAVFY 814
AmyAc_Glg_debranch cd11326
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
62-225 9.11e-08

Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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: 200465  Cd Length: 433  Bit Score: 54.78  E-value: 9.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A       62 YLTDMGVTAI-------WISQPVENVFSVMNdasgsasYHGYwardfkkpNP--FF-------------GTLSDFQRLVD 119
Cdd:cd11326  52 YLKELGVTAVellpvhaFDDEEHLVERGLTN-------YWGY--------NTlnFFapdpryasddapgGPVDEFKAMVK 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CYG_A      120 AAHAKGIKVIIDFAPNHTSPASETNPSYmeNGRLYDNGTllggY--TNDANMYFHHNGGT--TFssledgiyrnlfdlaD 195
Cdd:cd11326 117 ALHKAGIEVILDVVYNHTAEGGELGPTL--SFRGLDNAS----YyrLDPDGPYYLNYTGCgnTL---------------N 175
                       170       180       19