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Conserved domains on  [gi|62816022|emb|CAI46245|]
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cyclomaltodextrin glucanotransferase precursor [Haloferax mediterranei]

Protein Classification

alpha-amylase; alpha-amylase family glycosyl hydrolase( domain architecture ID 10183102)

alpha-amylase catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides| alpha-amylase family glycosyl hydrolase functions as a glycoside hydrolase that may act on starch, glycogen, and related oligo- and polysaccharides

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, ...
 47-431 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 [Multi-domain]  Cd Length: 389  Bit Score: 595.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  47 NFADDVIYQLISDRFRDGNPNNNPTG--ELASDDCSNLRKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITAVD- 123
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIe 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 124 SDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTsdgELEDGALYDNGSYVAAYNDDPK 203
Cdd:cd11320  79 GGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD---YAEDGALYDNGTLVGDYPNDDN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 204 SYFHHNGGT-DYSSYEDQIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPKWQKTLVDTIYDHRP 282
Cdd:cd11320 156 GWFHHNGGIdDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKP 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 283 VFTFGEWFLGADqsNPRYYE---FSNDSGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESEHDQVIDQVPFIDNHD 359
Cdd:cd11320 236 VFTFGEWFLGSP--DPGYEDyvkFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNHD 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 360 MPRFTVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTG----GNDPDNRKPMPSFDTTTTAYKVIQALTSLRSS 431
Cdd:cd11320 314 MPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGgtqvGGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 612-712 1.74e-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 [Multi-domain]  Cd Length: 101  Bit Score: 198.17  E-value: 1.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 612 DQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 62816022 692 SGSNRQYTTPTDSTGEYSGTW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 529-610 5.54e-26

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 [Multi-domain]  Cd Length: 81  Bit Score: 101.65  E-value: 5.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 529 PALGHVGPTMGQPGHTVVLSGDGFGSTEGSVEFGTTSASITSWSNTEIEATVPAVSGGYYDVTVTDANGAQSDPFSgYEV 608
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN-FEV 79


                ..
gi 62816022 609 LS 610
Cdd:cd00604  80 LT 81
Aamy_C smart00632
Aamy_C domain;
441-514 5.16e-14

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 67.65  E-value: 5.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62816022    441 EERWINSD-VFVYERefgDNVVLVAINRSlDWYDVSGLQTSLPEGTYDDALGGTLDGFSTTVNTDGsIDTFSVGP 514
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRS-DSDLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPA 70
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 47-431 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 [Multi-domain]  Cd Length: 389  Bit Score: 595.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  47 NFADDVIYQLISDRFRDGNPNNNPTG--ELASDDCSNLRKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITAVD- 123
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIe 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 124 SDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTsdgELEDGALYDNGSYVAAYNDDPK 203
Cdd:cd11320  79 GGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD---YAEDGALYDNGTLVGDYPNDDN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 204 SYFHHNGGT-DYSSYEDQIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPKWQKTLVDTIYDHRP 282
Cdd:cd11320 156 GWFHHNGGIdDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKP 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 283 VFTFGEWFLGADqsNPRYYE---FSNDSGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESEHDQVIDQVPFIDNHD 359
Cdd:cd11320 236 VFTFGEWFLGSP--DPGYEDyvkFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNHD 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 360 MPRFTVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTG----GNDPDNRKPMPSFDTTTTAYKVIQALTSLRSS 431
Cdd:cd11320 314 MPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGgtqvGGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 88-403 1.29e-72

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 238.80  E-value: 1.29e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022    88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFENitavdsdiGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS--------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVIL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   168 DFVPNHTSPstsdgeleDGALYDNgsyVAAYNDDPKS--YFHHNGGT-----------DYSSYED-------QIYRNLYN 227
Cdd:pfam00128  71 DLVVNHTSD--------EHAWFQE---SRSSKDNPYRdyYFWRPGGGpippnnwrsyfGGSAWTYdekgqeyYLHLFVAG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   228 LADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMP--------------PKWQKTLVDTIYDHRPVFTFGEWFLGA 293
Cdd:pfam00128 140 QPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISkvpglpfenngpfwHEFTQAMNETVFGYKDVMTVGEVFHGD 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   294 DQ-----SNPRYYEFSNdsGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESE-HDQVIDQVPFIDNHDMPRF-TVA 366
Cdd:pfam00128 220 GEwarvyTTEARMELEM--GFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDAlPDTNGWNFTFLGNHDQPRFlSRF 297

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 62816022   367 DGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDP 403
Cdd:pfam00128 298 GDDRASAKLLAVFLLTLRGTPYIYQGEEIGMTGGNDP 334
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
48-410 5.31e-71

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 237.07  E-value: 5.31e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  48 FADDVIYQLISDRFRDGNPnnnptgelasddcsnlrkYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITavdsdig 127
Cdd:COG0366   6 WKDAVIYQIYPDSFADSNG------------------DGGGDLKGIIEKL--DYLKDLGVDAIWLSPFFPSPM------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 128 tSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGSYVAAY--------N 199
Cdd:COG0366  59 -SDHGYDISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTS---DEHPWFQEARAGPDSPYRDWyvwrdgkpD 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 200 DDPKSYFHHNGG--TDYSSYEDQIYRNLYN--LADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPK------- 268
Cdd:COG0366 135 LPPNNWFSIFGGsaWTWDPEDGQYYLHLFFssQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDKDeglpenl 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 269 ------WQ--KTLVDTIYDHRpvFTFGEWFLGADQSNPRYyeFSNDSGMSLLDFRFGQEIRQVLRDFtdDWYGFRDMLQE 340
Cdd:COG0366 215 pevhefLRelRAAVDEYYPDF--FLVGEAWVDPPEDVARY--FGGDELDMAFNFPLMPALWDALAPE--DAAELRDALAQ 288

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62816022 341 TESEHDQVIDQVPFIDNHDMPRFTVADGDTRNTD---MALAVLLTSRGTPAVYYGTEQYLTGG--NDP----DNRKPMP 410
Cdd:COG0366 289 TPALYPEGGWWANFLRNHDQPRLASRLGGDYDRRrakLAAALLLTLPGTPYIYYGDEIGMTGDklQDPegrdGCRTPMP 367
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 612-712 1.74e-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 [Multi-domain]  Cd Length: 101  Bit Score: 198.17  E-value: 1.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 612 DQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 62816022 692 SGSNRQYTTPTDSTGEYSGTW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
Aamy smart00642
Alpha-amylase domain;
55-201 3.94e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 136.30  E-value: 3.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022     55 QLISDRFRDGNPNNnptgelasddcsnlrkycGGDWQGIIDKIQsgYLTDLGVSAVWISPPFENITAvdsdiGTSYHGYW 134
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESPQG-----YPSYHGYD 55

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62816022    135 ARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGSYVAAYNDD 201
Cdd:smart00642  56 ISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTS---DGGFRLDAAKFPLNGSAFSLLDF 119
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
 32-468 7.20e-35

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 140.53  E-value: 7.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   32 FVSQAAAATPPEQTVNFA------------DDVIYQLISDRFRDGNPNNN----------PTGELAS-------DDCSNL 82
Cdd:PRK10785  91 FTPQGFSRRPPARLEQFAvdvpdqgpqwvaDQVFYQIFPDRFARSLPREAvqdhvyyhhaAGQEIILrdwdepvTAQAGG 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   83 RKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFeniTAvdsdigTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNG 162
Cdd:PRK10785 171 STFYGGDLDGISEKL--PYLKKLGVTALYLNPIF---TA------PSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRG 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  163 IKVVIDFVPNHTSPSTS----DGELEDGALYDNGS-YVAAYNDDPKSYFHHNGGtdyssyedqiYRNLYNLaDFDHHE-- 235
Cdd:PRK10785 240 MRLVLDGVFNHTGDSHPwfdrHNRGTGGACHHPDSpWRDWYSFSDDGRALDWLG----------YASLPKL-DFQSEEvv 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  236 AYIDQYLKDAIKQWLDA--GIDGIRVDaVAHM-----PPKWQKTLVDTIYDhrpvftfgewflGADQSNPRYYefsndsg 308
Cdd:PRK10785 309 NEIYRGEDSIVRHWLKApyNIDGWRLD-VVHMlgeggGARNNLQHVAGITQ------------AAKEENPEAY------- 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  309 msLLDFRFGqEIRQVLRDFTDD----WYGF----RDMLQETE-SEHDQVID-------------QVPF---------IDN 357
Cdd:PRK10785 369 --VLGEHFG-DARQWLQADVEDaamnYRGFafplRAFLANTDiAYHPQQIDaqtcaawmdeyraGLPHqqqlrqfnqLDS 445

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  358 HDMPRF-TVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDPDNRKPMP----SFDTTTTAYkvIQALTSLRSSN 432
Cdd:PRK10785 446 HDTARFkTLLGGDKARMPLALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFPwdeaKQDGALLAL--YQRMIALRKKS 523

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 62816022  433 RRSPTADTEERWINSDVFVYEREFGDNVVLVAINRS 468
Cdd:PRK10785 524 QALRRGGCQVLYAEGNVVVFARVLQQQRVLVAINRG 559
CBM_20 pfam00686
Starch binding domain;
614-709 3.06e-31

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 117.00  E-value: 3.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   614 ISARFVVNdATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVhEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWESG 693
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYS-SYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESG 78

                          90
                  ....*....|....*.
gi 62816022   694 SNRQYTTPTDSTGEYS 709
Cdd:pfam00686  79 PNRSYTVPASGASTTT 94
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 529-610 5.54e-26

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 [Multi-domain]  Cd Length: 81  Bit Score: 101.65  E-value: 5.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 529 PALGHVGPTMGQPGHTVVLSGDGFGSTEGSVEFGTTSASITSWSNTEIEATVPAVSGGYYDVTVTDANGAQSDPFSgYEV 608
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN-FEV 79


                ..
gi 62816022 609 LS 610
Cdd:cd00604  80 LT 81
CBM_2 smart01065
Starch binding domain;
614-702 4.36e-23

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 93.57  E-value: 4.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022    614 ISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGpfFNQVVHEYPNWYYDVNLP-AGTDIEFKFVKIASDGTVTWES 692
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVP--LSPDTDGYPLWKGTVSLPpAGTTIEYKYVKVDEDGSVTWES 78

                           90
                   ....*....|
gi 62816022    693 GSNRQYTTPT 702
Cdd:smart01065  79 GPNRRLTVPE 88
Aamy_C smart00632
Aamy_C domain;
441-514 5.16e-14

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 67.65  E-value: 5.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62816022    441 EERWINSD-VFVYERefgDNVVLVAINRSlDWYDVSGLQTSLPEGTYDDALGGTLDGFSTTVNTDGsIDTFSVGP 514
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRS-DSDLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPA 70
trehalose_TreY TIGR02401
malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan ...
 101-173 3.27e-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 [Multi-domain]  Cd Length: 825  Bit Score: 60.11  E-value: 3.27e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022   101 YLTDLGVSAVWISPPFeniTAVdsdiGTSYHGYwarDFTDPNEF---FGDMETFKQLVDVAHQNGIKVVIDFVPNH 173
Cdd:TIGR02401  24 YLKSLGVSHLYLSPIL---TAV----PGSTHGY---DVVDHSEInpeLGGEEGLRRLSEAARARGLGLIVDIVPNH 89
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 444-523 9.89e-07

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 47.33  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   444 WIN-----SDVFVYEREFGDNVVLVAINRS-LDWYdvSGLQTSLPE-GTYDDAL-------GGTLDGFSTTVNTDG--SI 507
Cdd:pfam02806   1 WIDgddaeNNVIAFERGDDGGKLLVVFNFTpSVSY--TDYRTGLPEaGTYCEVLntddeeyGGSNTGEVVTVDGPGhpNS 78

                          90
                  ....*....|....*.
gi 62816022   508 DTFSVGPQTVCVWEHT 523
Cdd:pfam02806  79 LTLTLPPLSALVLKVE 94
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 534-600 1.34e-05

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: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 43.97  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62816022   534 VGPTMGQP--GHTVVLSGDGFG--STEGSVEFGTTSASITSWSNTEIEATVPAVSGGYYDVTVTDANGAQS 600
Cdd:pfam01833   6 ISPSSGPAsgGTTITITGSNFGtdSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIS 76
PLN02950 PLN02950
4-alpha-glucanotransferase
 607-710 5.97e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 46.64  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  607 EVLSGDQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRavGPFFNQVVHeyPNWYYDVNLPAGT-DIEFKFVKIASD 685
Cdd:PLN02950 146 KPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDD--GLKLNYTGD--SIWEADCLVPKSDfPIKYKYALQTAE 221

                         90       100
                 ....*....|....*....|....*
gi 62816022  686 GTVTWESGSNRQYTTPTDSTGEYSG 710
Cdd:PLN02950 222 GLVSLELGVNRELSLDSSSGKPPSY 246
 
Name Accession Description Interval E-value
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 47-431 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 [Multi-domain]  Cd Length: 389  Bit Score: 595.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  47 NFADDVIYQLISDRFRDGNPNNNPTG--ELASDDCSNLRKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITAVD- 123
Cdd:cd11320   1 DFETDVIYQILTDRFYDGDTSNNPPGspGLYDPTHSNLKKYWGGDWQGIIDKL--PYLKDLGVTAIWISPPVENINSPIe 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 124 SDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTsdgELEDGALYDNGSYVAAYNDDPK 203
Cdd:cd11320  79 GGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNHSSPAD---YAEDGALYDNGTLVGDYPNDDN 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 204 SYFHHNGGT-DYSSYEDQIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPKWQKTLVDTIYDHRP 282
Cdd:cd11320 156 GWFHHNGGIdDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKP 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 283 VFTFGEWFLGADqsNPRYYE---FSNDSGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESEHDQVIDQVPFIDNHD 359
Cdd:cd11320 236 VFTFGEWFLGSP--DPGYEDyvkFANNSGMSLLDFPLNQAIRDVFAGFTATMYDLDAMLQQTSSDYNYENDLVTFIDNHD 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 360 MPRFTVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTG----GNDPDNRKPMPSFDTTTTAYKVIQALTSLRSS 431
Cdd:cd11320 314 MPRFLTLNNNDKRLHQALAFLLTSRGIPVIYYGTEQYLHGgtqvGGDPYNRPMMPSFDTTTTAYKLIKKLADLRKS 389
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 49-432 2.06e-77

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


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 251.79  E-value: 2.06e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  49 ADDVIYQLISDRFRDGNPNNN---PTGELASDDCSNlRKYCGGDWQGIIDKIQsgYLTDLGVSAVWISPPFENitAVDSD 125
Cdd:cd11339   1 REETIYFVMTDRFYDGDPSNDnggGDGDPRSNPTDN-GPYHGGDFKGLIDKLD--YIKDLGFTAIWITPVVKN--RSVQA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 126 IGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstsdgeledgalydngsyvaaynddpksy 205
Cdd:cd11339  76 GSAGYHGYWGYDFYRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG------------------------------ 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 206 fhhnggtdyssyedqiyrnlynlaDFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPKWQKTLVDTIYD---HRP 282
Cdd:cd11339 126 ------------------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQaagKPD 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 283 VFTFGEWFLGaDQSNPRYYeFSNDSGMSLLDFRFGQEIRQVLRDFT-----DDWYGfRDMLQETESEhdqvidQVPFIDN 357
Cdd:cd11339 182 FFMFGEVYDG-DPSYIAPY-TTTAGGDSVLDFPLYGAIRDAFAGGGsgdllQDLFL-SDDLYNDATE------LVTFLDN 252

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 358 HDMPRF-----TVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDPDNRKPMP------------SFDTTTTAYK 420
Cdd:cd11339 253 HDMGRFlsslkDGSADGTARLALALALLFTSRGIPCIYYGTEQGFTGGGDPDNGRRNMfastgdltsaddNFDTDHPLYQ 332

                       410
                ....*....|..
gi 62816022 421 VIQALTSLRSSN 432
Cdd:cd11339 333 YIARLNRIRRAY 344
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 88-403 1.29e-72

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 238.80  E-value: 1.29e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022    88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFENitavdsdiGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:pfam00128   1 GDLQGIIEKLD--YLKELGVTAIWLSPIFDS--------PQADHGYDIADYYKIDPHYGTMEDFKELISKAHERGIKVIL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   168 DFVPNHTSPstsdgeleDGALYDNgsyVAAYNDDPKS--YFHHNGGT-----------DYSSYED-------QIYRNLYN 227
Cdd:pfam00128  71 DLVVNHTSD--------EHAWFQE---SRSSKDNPYRdyYFWRPGGGpippnnwrsyfGGSAWTYdekgqeyYLHLFVAG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   228 LADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMP--------------PKWQKTLVDTIYDHRPVFTFGEWFLGA 293
Cdd:pfam00128 140 QPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISkvpglpfenngpfwHEFTQAMNETVFGYKDVMTVGEVFHGD 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   294 DQ-----SNPRYYEFSNdsGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESE-HDQVIDQVPFIDNHDMPRF-TVA 366
Cdd:pfam00128 220 GEwarvyTTEARMELEM--GFNFPHNDVALKPFIKWDLAPISARKLKEMITDWLDAlPDTNGWNFTFLGNHDQPRFlSRF 297

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 62816022   367 DGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDP 403
Cdd:pfam00128 298 GDDRASAKLLAVFLLTLRGTPYIYQGEEIGMTGGNDP 334
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
48-410 5.31e-71

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 237.07  E-value: 5.31e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  48 FADDVIYQLISDRFRDGNPnnnptgelasddcsnlrkYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITavdsdig 127
Cdd:COG0366   6 WKDAVIYQIYPDSFADSNG------------------DGGGDLKGIIEKL--DYLKDLGVDAIWLSPFFPSPM------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 128 tSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGSYVAAY--------N 199
Cdd:COG0366  59 -SDHGYDISDYRDVDPRFGTLADFDELVAEAHARGIKVILDLVLNHTS---DEHPWFQEARAGPDSPYRDWyvwrdgkpD 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 200 DDPKSYFHHNGG--TDYSSYEDQIYRNLYN--LADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHMPPK------- 268
Cdd:COG0366 135 LPPNNWFSIFGGsaWTWDPEDGQYYLHLFFssQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDKDeglpenl 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 269 ------WQ--KTLVDTIYDHRpvFTFGEWFLGADQSNPRYyeFSNDSGMSLLDFRFGQEIRQVLRDFtdDWYGFRDMLQE 340
Cdd:COG0366 215 pevhefLRelRAAVDEYYPDF--FLVGEAWVDPPEDVARY--FGGDELDMAFNFPLMPALWDALAPE--DAAELRDALAQ 288

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62816022 341 TESEHDQVIDQVPFIDNHDMPRFTVADGDTRNTD---MALAVLLTSRGTPAVYYGTEQYLTGG--NDP----DNRKPMP 410
Cdd:COG0366 289 TPALYPEGGWWANFLRNHDQPRLASRLGGDYDRRrakLAAALLLTLPGTPYIYYGDEIGMTGDklQDPegrdGCRTPMP 367
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 52-431 1.36e-63

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


Pssm-ID: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 216.28  E-value: 1.36e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRF-RDGNPNNNPtgelasddCSNL-RKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITAVDSDiGTS 129
Cdd:cd11319  10 SIYQVLTDRFaRTDGSSTAP--------CDTAdRTYCGGTWKGIINKL--DYIQGMGFDAIWISPIVKNIEGNTAY-GEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 130 YHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDgalyDNGSYVAAYNDdpKSYFHH- 208
Cdd:cd11319  79 YHGYWAQDLYSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMA---SAGPGSD----VDYSSFVPFND--SSYYHPy 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 209 ---NGGTDYSSYED-QIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDA-GIDGIRVDAVAHMPPKWQKTLVDTIydhrPV 283
Cdd:cd11319 150 cwiTDYNNQTSVEDcWLGDDVVALPDLNTENPFVVSTLNDWIKNLVSNySIDGLRIDTAKHVRKDFWPGFVEAA----GV 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 284 FTFGEWFLGadqsNPRY---YEFSNDsgmSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQeteSEHDQVIDQ---VPFIDN 357
Cdd:cd11319 226 FAIGEVFDG----DPNYvcpYQNYLD---GVLNYPLYYPLVDAFQSTKGSMSALVDTIN---SVQSSCKDPtllGTFLEN 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 358 HDMPRFTvadgdTRNTDM-----ALAVLLTSRGTPAVYYGTEQYLTGGNDPDNRKPM-PS-FDTTTTAYKVIQALTSLRS 430
Cdd:cd11319 296 HDNPRFL-----SYTSDQalaknALAFTLLSDGIPIIYYGQEQGFNGGNDPYNREALwLSgYDTSSPLYKFIKTLNAIRK 370


                .
gi 62816022 431 S 431
Cdd:cd11319 371 A 371
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 612-712 1.74e-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 [Multi-domain]  Cd Length: 101  Bit Score: 198.17  E-value: 1.74e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 612 DQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWE 691
Cdd:cd05807   1 DQVSVRFVVNNATTQLGENVYLVGNVHELGNWDPSKAIGPFFNQVVYQYPNWYYDVSVPAGTTIEFKFIKKNGDNTVTWE 80

                        90       100
                ....*....|....*....|.
gi 62816022 692 SGSNRQYTTPTDSTGEYSGTW 712
Cdd:cd05807  81 SGSNHTYTAPSSTTGTIRVNW 101
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 52-433 2.60e-54

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 [Multi-domain]  Cd Length: 389  Bit Score: 191.54  E-value: 2.60e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRFRDGNPNNNPT-GELASDDCSNLRKYC-------------GGDWQGIIDKIqsGYLTDLGVSAVWISPPFE 117
Cdd:cd11338   3 VFYQIFPDRFANGDPSNDPKgGEYNYFGWPDLPDYPppwggeptrrdfyGGDLQGIIEKL--DYLKDLGVNAIYLNPIFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 118 nitavdsdiGTSYHGYWARDFT--DPNefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpSTS---DGELEDGalyDNG 192
Cdd:cd11338  81 ---------APSNHKYDTADYFkiDPH--LGTEEDFKELVEEAHKRGIRVILDGVFNHTG-DDSpyfQDVLKYG---ESS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 193 SYvaaynddpKSYFHHNGGTDYSSYEDQIYR---NLYNLADFDH-HEAYIDqYLKDAIKQWLDAG-IDGIRVDaVAHM-P 266
Cdd:cd11338 146 AY--------QDWFSIYYFWPYFTDEPPNYEswwGVPSLPKLNTeNPEVRE-YLDSVARYWLKEGdIDGWRLD-VADEvP 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 267 PKWQKTLVDTIYDHRP-VFTFGE-------WFLGaDQS----NpryYEFSNdsgmSLLDFrfgqeirqvLRDFTDDWYGF 334
Cdd:cd11338 216 HEFWREFRKAVKAVNPdAYIIGEvwedarpWLQG-DQFdsvmN---YPFRD----AVLDF---------LAGEEIDAEEF 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 335 RDMLQETESEH-DQVID-QVPFIDNHDMPRF-TVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDPDNRKPMP- 410
Cdd:cd11338 279 ANRLNSLRANYpKQVLYaMMNLLDSHDTPRIlTLLGGDKARLKLALALQFTLPGAPCIYYGDEIGLEGGKDPDNRRPMPw 358

                       410       420
                ....*....|....*....|....*.
gi 62816022 411 ---SFDTTTTAYkvIQALTSLRSSNR 433
Cdd:cd11338 359 deeKWDQDLLEF--YKKLIALRKEHP 382
AmyAc_bac_CMD_like_3 cd11340
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 49-410 1.58e-53

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 [Multi-domain]  Cd Length: 407  Bit Score: 189.73  E-value: 1.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  49 ADDVIYQLISDRFRDGNP-NNNPTGELASDDCSNLRKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENitavdSDIG 127
Cdd:cd11340   2 SSDVIYLIMPDRFANGDPsNDSVPGMLEKADRSNPNGRHGGDIQGIIDHL--DYLQDLGVTAIWLTPLLEN-----DMPS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 128 TSYHGYWARDF--TDPNefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTspstsdgeledgalydnGSYVAAYNDDP-KS 204
Cdd:cd11340  75 YSYHGYAATDFyrIDPR--FGSNEDYKELVSKAHARGMKLIMDMVPNHC-----------------GSEHWWMKDLPtKD 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 205 YFHHNGGTDYSSYEDQIYRNLY----------------NLADFDHHEAYIDQYLKDAIKQWLD-AGIDGIRVD----AVA 263
Cdd:cd11340 136 WINQTPEYTQTNHRRTALQDPYasqadrklfldgwfvpTMPDLNQRNPLVARYLIQNSIWWIEyAGLDGIRVDtypySDK 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 264 HMPPKWQKTlvdtIYDHRPVFT-FGEWFLG---------ADQSNPRYYefsnDSGM-SLLDFRFGQEIRQVLRDfTDDWY 332
Cdd:cd11340 216 DFMSEWTKA----IMEEYPNFNiVGEEWSGnpaivaywqKGKKNPDGY----DSHLpSVMDFPLQDALRDALNE-EEGWD 286

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 333 GFRDMLQETESeHDQVI----DQVPFIDNHDMPRF-TVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGN---DPD 404
Cdd:cd11340 287 TGLNRLYETLA-NDFLYpdpnNLVIFLDNHDTSRFySQVGEDLDKFKLALALLLTTRGIPQLYYGTEILMKGTKkkdDGA 365


                ....*.
gi 62816022 405 NRKPMP 410
Cdd:cd11340 366 IRRDFP 371
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 52-391 3.03e-47

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


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 168.12  E-value: 3.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRFRDGNPNNNptgelasddcsnlrkYCGGDWQGIIDKIQsgYLTDLGVSAVWISPPFENitavdSDIGTSYH 131
Cdd:cd00551   1 VIYQLFPDRFTDGDSSGG---------------DGGGDLKGIIDKLD--YLKDLGVTAIWLTPIFES-----PEYDGYDK 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 132 GYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHtspstsdgeledgalydngsyvaaynddpksyfhhngg 211
Cdd:cd00551  59 DDGYLDYYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 212 tdyssyedqiyrnlynladfdhheayidqylkDAIKQWLDAGIDGIRVDAVAHMPPKWQKTLVDTIYDHRP-----VFTF 286
Cdd:cd00551 101 --------------------------------DILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREIRKDAKlakpdTLLL 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 287 GEWFLGADQSNPRYYEfsNDSGMSLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETesehDQVIDQVPFIDNHDMPRF--- 363
Cdd:cd00551 149 GEAWGGPDELLAKAGF--DDGLDSVFDFPLLEALRDALKGGEGALAILAALLLLN----PEGALLVNFLGNHDTFRLadl 222

                       330       340       350
                ....*....|....*....|....*....|.
gi 62816022 364 ---TVADGDTRNTDMALAVLLTSRGTPAVYY 391
Cdd:cd00551 223 vsyKIVELRKARLKLALALLLTLPGTPMIYY 253
AmyAc_5 cd11352
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 52-428 2.76e-42

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 [Multi-domain]  Cd Length: 443  Bit Score: 159.40  E-value: 2.76e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRFRDG-------NPNNNPTGELASDDC---SNLRKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITA 121
Cdd:cd11352   1 VLYFLLVDRFSDGkerprplFDGNDPAVATWEDNFgweSQGQRFQGGTLKGVRSKL--GYLKRLGVTALWLSPVFKQRPE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 122 VDSdigtsYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTSdGELEDGALYDNGSYVAAYNDD 201
Cdd:cd11352  79 LET-----YHGYGIQNFLDVDPRFGTREDLRDLVDAAHARGIYVILDIILNHSGDVFS-YDDDRPYSSSPGYYRGFPNYP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 202 PKSYFHHNGGTDY--SSYEDQIY----RNL-----------------------YNLADFDH------HEAYIDqyLKDAI 246
Cdd:cd11352 153 PGGWFIGGDQDALpeWRPDDAIWpaelQNLeyytrkgrirnwdgypeykegdfFSLKDFRTgsgsipSAALDI--LARVY 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 247 KQWLD-AGIDGIRVDAVAHMPPKWQKTLVDTIYDH------RPVFTFGEwfLGADQSNPRyYEFSNDSGM-SLLDFrfgQ 318
Cdd:cd11352 231 QYWIAyADIDGFRIDTVKHMEPGAARYFCNAIKEFaqsigkDNFFLFGE--ITGGREAAA-YEDLDVTGLdAALDI---P 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 319 EIRQVLRDFTDDWY-------GFRDMLQETESEHDQVIDQ-VPFIDNHDM-----PRFTVADgdtRNTD----MALAVLL 381
Cdd:cd11352 305 EIPFKLENVAKGLAppaeyfqLFENSKLVGMGSHRWYGKFhVTFLDDHDQvgrfyKKRRAAD---AAGDaqlaAALALNL 381

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62816022 382 TSRGTPAVYYGTEQYLTGGNDPDN--RKPM-----PSFDTTTT--------AYKVIQALTSL 428
Cdd:cd11352 382 FTLGIPCIYYGTEQGLDGSGDSDRyvREAMfggdfGAFRSRGRhffneehpIYRRIAALSEL 443
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 88-410 5.20e-39

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


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 149.27  E-value: 5.20e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFEnitavdsdiGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:cd11316  20 GDLNGLTEKLD--YLNDLGVNGIWLMPIFP---------SPSYHGYDVTDYYAIEPDYGTMEDFERLIAEAHKRGIKVII 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 168 DFVPNHTSpstSDGEL-EDGALYDNGSYVAAYN---DDPKSYFHHNGGTDYSSYEDQIYRNLY--NLADFDHHEAYIDQY 241
Cdd:cd11316  89 DLVINHTS---SEHPWfQEAASSPDSPYRDYYIwadDDPGGWSSWGGNVWHKAGDGGYYYGAFwsGMPDLNLDNPAVREE 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 242 LKDAIKQWLDAGIDGIRVDAVAHMPP---------------KWQKTLVDTIYDHrpVFTFGE-WflgADQSNP-RYYEFS 304
Cdd:cd11316 166 IKKIAKFWLDKGVDGFRLDAAKHIYEngegqadqeeniefwKEFRDYVKSVKPD--AYLVGEvW---DDPSTIaPYYASG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 305 NDsgmSLLDFRFGQEIRQVLRDfTDDWYGFRDMLQETESEHDQVIDQV---PFIDNHDMPR-FTVADGDTRNTDMALAVL 380
Cdd:cd11316 241 LD---SAFNFDLAEAIIDSVKN-GGSGAGLAKALLRVYELYAKYNPDYidaPFLSNHDQDRvASQLGGDEAKAKLAAALL 316

                       330       340       350
                ....*....|....*....|....*....|.
gi 62816022 381 LTSRGTPAVYYGTEQYLTG-GNDPDNRKPMP 410
Cdd:cd11316 317 LTLPGNPFIYYGEEIGMLGsKPDENIRTPMS 347
Aamy smart00642
Alpha-amylase domain;
55-201 3.94e-37

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 136.30  E-value: 3.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022     55 QLISDRFRDGNPNNnptgelasddcsnlrkycGGDWQGIIDKIQsgYLTDLGVSAVWISPPFENITAvdsdiGTSYHGYW 134
Cdd:smart00642   1 QIYPDRFADGNGDG------------------GGDLQGIIEKLD--YLKDLGVTAIWLSPIFESPQG-----YPSYHGYD 55

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62816022    135 ARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGSYVAAYNDD 201
Cdd:smart00642  56 ISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDVVINHTS---DGGFRLDAAKFPLNGSAFSLLDF 119
PRK10785 PRK10785
maltodextrin glucosidase; Provisional
 32-468 7.20e-35

maltodextrin glucosidase; Provisional


Pssm-ID: 236759 [Multi-domain]  Cd Length: 598  Bit Score: 140.53  E-value: 7.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   32 FVSQAAAATPPEQTVNFA------------DDVIYQLISDRFRDGNPNNN----------PTGELAS-------DDCSNL 82
Cdd:PRK10785  91 FTPQGFSRRPPARLEQFAvdvpdqgpqwvaDQVFYQIFPDRFARSLPREAvqdhvyyhhaAGQEIILrdwdepvTAQAGG 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   83 RKYCGGDWQGIIDKIqsGYLTDLGVSAVWISPPFeniTAvdsdigTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNG 162
Cdd:PRK10785 171 STFYGGDLDGISEKL--PYLKKLGVTALYLNPIF---TA------PSVHKYDTEDYRHVDPQLGGDAALLRLRHATQQRG 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  163 IKVVIDFVPNHTSPSTS----DGELEDGALYDNGS-YVAAYNDDPKSYFHHNGGtdyssyedqiYRNLYNLaDFDHHE-- 235
Cdd:PRK10785 240 MRLVLDGVFNHTGDSHPwfdrHNRGTGGACHHPDSpWRDWYSFSDDGRALDWLG----------YASLPKL-DFQSEEvv 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  236 AYIDQYLKDAIKQWLDA--GIDGIRVDaVAHM-----PPKWQKTLVDTIYDhrpvftfgewflGADQSNPRYYefsndsg 308
Cdd:PRK10785 309 NEIYRGEDSIVRHWLKApyNIDGWRLD-VVHMlgeggGARNNLQHVAGITQ------------AAKEENPEAY------- 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  309 msLLDFRFGqEIRQVLRDFTDD----WYGF----RDMLQETE-SEHDQVID-------------QVPF---------IDN 357
Cdd:PRK10785 369 --VLGEHFG-DARQWLQADVEDaamnYRGFafplRAFLANTDiAYHPQQIDaqtcaawmdeyraGLPHqqqlrqfnqLDS 445

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  358 HDMPRF-TVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTGGNDPDNRKPMP----SFDTTTTAYkvIQALTSLRSSN 432
Cdd:PRK10785 446 HDTARFkTLLGGDKARMPLALVWLFTWPGVPCIYYGDEVGLDGGNDPFCRKPFPwdeaKQDGALLAL--YQRMIALRKKS 523

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 62816022  433 RRSPTADTEERWINSDVFVYEREFGDNVVLVAINRS 468
Cdd:PRK10785 524 QALRRGGCQVLYAEGNVVVFARVLQQQRVLVAINRG 559
CBM_20 pfam00686
Starch binding domain;
614-709 3.06e-31

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 117.00  E-value: 3.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   614 ISARFVVNdATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVhEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWESG 693
Cdd:pfam00686   1 VSVTFNVN-ATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYS-SYPLWSGTVSLPAGTTIEYKYIKVDSDGSVTWESG 78

                          90
                  ....*....|....*.
gi 62816022   694 SNRQYTTPTDSTGEYS 709
Cdd:pfam00686  79 PNRSYTVPASGASTTT 94
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
 81-432 3.79e-31

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 [Multi-domain]  Cd Length: 336  Bit Score: 124.58  E-value: 3.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  81 NLRKYCG-GDWQGIIDKIQsgYLTDLGVSAVWISPPFEniTAVDSDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAH 159
Cdd:cd11313  11 NVRQFTPeGTFKAVTKDLP--RLKDLGVDILWLMPIHP--IGEKNRKGSLGSPYAVKDYRAVNPEYGTLEDFKALVDEAH 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 160 QNGIKVVIDFVPNHTSPstsdgeledgalyDNgsyvAAYNDDPKSYFHHNGGTDYSSYEDqiYRNLYNLaDFDHHEayID 239
Cdd:cd11313  87 DRGMKVILDWVANHTAW-------------DH----PLVEEHPEWYLRDSDGNITNKVFD--WTDVADL-DYSNPE--LR 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 240 QYLKDAIKQWLD-AGIDGIRVDaVAHMPPK--WQKT--LVDTIydHRPVFTFGEWflgadqSNPRYYEFsndsgMSLLDF 314
Cdd:cd11313 145 DYMIDAMKYWVReFDVDGFRCD-VAWGVPLdfWKEAraELRAV--KPDVFMLAEA------EPRDDDEL-----YSAFDM 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 315 RFGQEIRQVLRDF---TDDWYGFRDMLQETESEHDQVIDQVPFIDNHDMPRFTVADGDTRNTDMALAVLLTSRGTPAVYY 391
Cdd:cd11313 211 TYDWDLHHTLNDVakgKASASDLLDALNAQEAGYPKNAVKMRFLENHDENRWAGTVGEGDALRAAAALSFTLPGMPLIYN 290

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 62816022 392 GTEQYLTGGNDPDNRKPMPSFDT-TTTAYkvIQALTSLRSSN 432
Cdd:cd11313 291 GQEYGLDKRPSFFEKDPIDWTKNhDLTDL--YQKLIALKKEN 330
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
 613-713 2.15e-29

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: 112.31  E-value: 2.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 613 QISARFVV-NDATTDVGENVYVVGNVHELGDW--DTDRAVGPFfnqVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVT 689
Cdd:cd05820   2 QIPVIFTVqNTPETAPGEFLYLTGSVPELGNWstSTDQAVGPL---LCPNWPDWFVVASVPAGTYIEFKFLKAPADGTGT 78

                        90       100
                ....*....|....*....|....
gi 62816022 690 WESGSNRQYTTPTDSTGEYSGTWK 713
Cdd:cd05820  79 WEGGSNHAYTTPSGGTGTVTVTWQ 102
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 101-436 4.21e-28

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


Pssm-ID: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 116.27  E-value: 4.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFENITavdsdigtsyHGYWARDF--TDPNefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTS--- 175
Cdd:cd11354  39 YAVELGCNGLLLGPVFESAS----------HGYDTLDHyrIDPR--LGDDEDFDALIAAAHERGLRVLLDGVFNHVGrsh 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 176 PSTSDGeLEDGAlydngsyvaayNDDPKSYFHHNGGTDYSSYEDQiyrnlYNLADFDHHEAYIDQYLKDAIKQWLDAGID 255
Cdd:cd11354 107 PAVAQA-LEDGP-----------GSEEDRWHGHAGGGTPAVFEGH-----EDLVELDHSDPAVVDMVVDVMCHWLDRGID 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 256 GIRVDAVAHMPPK-WQKTLVDTIYDHRPVFTFGEWFLGadqsnpRYYEFSNDSGM-SLLDFRFGQEIRQVLRD---FTDD 330
Cdd:cd11354 170 GWRLDAAYAVPPEfWARVLPRVRERHPDAWILGEVIHG------DYAGIVAASGMdSVTQYELWKAIWSSIKDrnfFELD 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 331 WygfrdmlqeTESEHDQVIDQ-VP--FIDNHDMPRFTVADGDtRNTDMALAVLLTSRGTPAVYYGTEQYLTG------GN 401
Cdd:cd11354 244 W---------ALGRHNEFLDSfVPqtFVGNHDVTRIASQVGD-DGAALAAAVLFTVPGIPSIYYGDEQGFTGvkeeraGG 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 62816022 402 DPDNRKPMP-SFDTTTTA----YKVIQALTSLRssnRRSP 436
Cdd:cd11354 314 DDAVRPAFPaSPAELAPLgewiYRLHQDLIGLR---RRHP 350
malS PRK09505
alpha-amylase; Reviewed
 38-394 2.69e-27

alpha-amylase; Reviewed


Pssm-ID: 236543 [Multi-domain]  Cd Length: 683  Bit Score: 117.85  E-value: 2.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   38 AATPPEQTVNFADDVIYQLISDRFRDGNPNNNPTGELASDDCSNLRKYCGGDWQGIIDKIQsgYLTDLGVSAVWISPPFE 117
Cdd:PRK09505 177 AETEAAAPFDWHNATVYFVLTDRFENGDPSNDHSYGRHKDGMQEIGTFHGGDLRGLTEKLD--YLQQLGVNALWISSPLE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  118 NITA-VDSdiGTS-------YHGYWARDFT--DPNefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPST-SD-GELED 185
Cdd:PRK09505 255 QIHGwVGG--GTKgdfphyaYHGYYTLDWTklDAN--MGTEADLRTLVDEAHQRGIRILFDVVMNHTGYATlADmQEFQF 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  186 GALYDNGSYVAAY-----ND-DPK------SY-----FHHNGG-----------TDYSSYE----DQIYRNLYNLADF-- 231
Cdd:PRK09505 331 GALYLSGDENKKTlgerwSDwQPAagqnwhSFndyinFSDSTAwdkwwgkdwirTDIGDYDnpgfDDLTMSLAFLPDIkt 410

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  232 ----------------DHHEAYIDQYLK-DAIKQWL-----DAGIDGIRVDAVAHMPP---------------KWQKTLV 274
Cdd:PRK09505 411 estqasglpvfyankpDTRAKAIDGYTPrDYLTHWLsqwvrDYGIDGFRVDTAKHVELpawqqlkqeasaalaEWKKANP 490

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  275 DTIYDHRPVFTFGE-WFLGADQSNprYYefsnDSGM-SLLDFRFGQEIRQVLRDFTDDWYGFRDMLQETESEHdqvidQV 352
Cdd:PRK09505 491 DKALDDAPFWMTGEaWGHGVMKSD--YY----RHGFdAMINFDYQEQAAKAVDCLAQMDPTYQQMAEKLQDFN-----VL 559

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 62816022  353 PFIDNHDMPRFTVADGDTRNTDMALAVLLTSRGTPAVYYGTE 394
Cdd:PRK09505 560 SYLSSHDTRLFFEGGQSYAKQRRAAELLLLAPGAVQIYYGDE 601
AmyAc_SI_OligoGlu_DGase cd11333
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ...
 88-410 3.56e-27

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 [Multi-domain]  Cd Length: 428  Bit Score: 114.86  E-value: 3.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIqsGYLTDLGVSAVWISP----PFenitaVDsdigtsyHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGI 163
Cdd:cd11333  22 GDLPGIISKL--DYLKDLGVDAIWLSPiypsPQ-----VD-------NGYDISDYRAIDPEFGTMEDFDELIKEAHKRGI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 164 KVVIDFVPNHTS---P----STSDGeledgalyDNgsyvaAYND-----DPK---------SYFhhnGGtdyS--SYEDQ 220
Cdd:cd11333  88 KIIMDLVVNHTSdehPwfqeSRSSR--------DN-----PYRDyyiwrDGKdgkppnnwrSFF---GG---SawEYDPE 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 221 iyRNLYNLADFDHHEAyiD---------QYLKDAIKQWLDAGIDGIRVDAVAH---------MPPK-------------- 268
Cdd:cd11333 149 --TGQYYLHLFAKEQP--DlnwenpevrQEIYDMMRFWLDKGVDGFRLDVINLiskdpdfpdAPPGdgdglsghkyyang 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 269 -----WQKTLVDTIYDHRPVFTFGE-WFLGADQSnPRYYEFSNDS-----GMSLLDFRFGQEIRQVLRDFtdDWYGFRDM 337
Cdd:cd11333 225 pgvheYLQELNREVFSKYDIMTVGEaPGVDPEEA-LKYVGPDRGElsmvfNFEHLDLDYGPGGKWKPKPW--DLEELKKI 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 338 LQETESEHDQVIDQVPFIDNHDMPR----FtvADGDTRNTDMA--LA-VLLTSRGTPAVYYGTEQYLTggNDPDN-RKPM 409
Cdd:cd11333 302 LSKWQKALQGDGWNALFLENHDQPRsvsrF--GNDGEYRVESAkmLAtLLLTLRGTPFIYQGEEIGMT--NSRDNaRTPM 377


                .
gi 62816022 410 P 410
Cdd:cd11333 378 Q 378
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 614-713 7.28e-27

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: 104.75  E-value: 7.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 614 ISARFVVNdATTDVGENVYVVGNVHELGDWDTDRAV--GPFfnqvvhEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWE 691
Cdd:cd05808   1 VAVTFNVT-ATTVWGQNVYVVGNVPELGNWSPANAValSAA------TYPVWSGTVDLPAGTAIEYKYIKKDGSGTVTWE 73

                        90       100
                ....*....|....*....|..
gi 62816022 692 SGSNRQYTTPTDSTGEYSGTWK 713
Cdd:cd05808  74 SGPNRTATTPASGTLTLNDTWR 95
AmyAc_CMD_like cd11337
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 101-436 1.02e-26

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 [Multi-domain]  Cd Length: 328  Bit Score: 111.46  E-value: 1.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFEnitavdsdigTSYHGYWARDFT--DPNefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpst 178
Cdd:cd11337  36 HLKELGCNALYLGPVFE----------SDSHGYDTRDYYriDRR--LGTNEDFKALVAALHERGIRVVLDGVFNHVG--- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 179 sdgeledgalydngsyvaaynddpKSYF---HhnggtdyssyedqiyrnlYNLADFDHHEAYIDQYLKDAIKQWLDAG-I 254
Cdd:cd11337 101 ------------------------RDFFwegH------------------YDLVKLNLDNPAVVDYLFDVVRFWIEEFdI 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 255 DGIRVDAVAHMPPKWQKTLVDTIYDHRPVFtfgeWFLG----ADqsnprYYEFSNDSGM-SLLDFrfgqEIRQVLrdftd 329
Cdd:cd11337 139 DGLRLDAAYCLDPDFWRELRPFCRELKPDF----WLMGevihGD-----YNRWVNDSMLdSVTNY----ELYKGL----- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 330 dWYGFRDM--------LQETESEHDQVIDQVP--FIDNHDMPRFTVADGDTRNTDMALAVLLTSRGTPAVYYGTEQYLTG 399
Cdd:cd11337 201 -WSSHNDHnffeiahsLNRLFRHNGLYRGFHLytFVDNHDVTRIASILGDKAHLPLAYALLFTMPGIPSIYYGSEWGIEG 279

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 62816022 400 ----GNDPDNRKPMPSFDTTTTA----YKVIQALTSLRssnRRSP 436
Cdd:cd11337 280 vkeeGSDADLRPLPLRPAELSPLgnelTRLIQALIALR---RRSP 321
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 617-712 2.47e-26

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: 103.15  E-value: 2.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 617 RFVVNdATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQvvhEYPNWYYDVNLPA--GTDIEFKFVKIASDGTVTWESGS 694
Cdd:cd05467   3 RFQVR-CTTQFGQSVYVVGSHPELGNWDPAKALRLNTSN---SYPLWTGEIPLPApeGQVIEYKYVIVDDDGNVQWESGS 78

                        90
                ....*....|....*...
gi 62816022 695 NRQYTTPTDSTGEYSGTW 712
Cdd:cd05467  79 NRVLTVPSTSSLIVVDDW 96
IPT_CGTD cd00604
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ...
 529-610 5.54e-26

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 [Multi-domain]  Cd Length: 81  Bit Score: 101.65  E-value: 5.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 529 PALGHVGPTMGQPGHTVVLSGDGFGSTEGSVEFGTTSASITSWSNTEIEATVPAVSGGYYDVTVTDANGAQSDPFSgYEV 608
Cdd:cd00604   1 PLIGSVGPVMGKPGNTVTISGEGFGSTGGTVYFGGTAAEVLSWSDTSIVVEVPRVAPGNYNISVTTVDGVTSNGYN-FEV 79


                ..
gi 62816022 609 LS 610
Cdd:cd00604  80 LT 81
AmyAc_SLC3A1 cd11359
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ...
 50-409 7.18e-26

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 [Multi-domain]  Cd Length: 456  Bit Score: 111.30  E-value: 7.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  50 DDVIYQLISDRFRDGNPNNNptgelasddcsnlrkycgGDWQGIIDKIqsGYLTDLGVSAVWISPPFENiTAVDsdigts 129
Cdd:cd11359   5 TSVIYQIYPRSFKDSNGDGN------------------GDLKGIREKL--DYLKYLGVKTVWLSPIYKS-PMKD------ 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 130 yHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTS--------PSTSDGELEDGALYDNGsyVAAYNDD 201
Cdd:cd11359  58 -FGYDVSDFTDIDPMFGTMEDFERLLAAMHDRGMKLIMDFVPNHTSdkhewfqlSRNSTNPYTDYYIWADC--TADGPGT 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 202 P----KSYFhhnGGTDYsSYEDQiyRNLYNLADFDHHEAYID-------QYLKDAIKQWLDAGIDGIRVDAVAHM----- 265
Cdd:cd11359 135 PpnnwVSVF---GNSAW-EYDEK--RNQCYLHQFLKEQPDLNfrnpdvqQEMDDVLRFWLDKGVDGFRVDAVKHLleath 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 266 ------PPKWQKTL-VDTIYDHRPVFTFG---------EWFLGADQ--SNPRYYEF-------SNDSGMSLLDFRFGQE- 319
Cdd:cd11359 209 lrdepqVNPTQPPEtQYNYSELYHDYTTNqegvhdiirDWRQTMDKysSEPGRYRFmitevydDIDTTMRYYGTSFKQEa 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 320 ---IRQVLRDFTDDWYGfrdmlQETESEHDQVIDQVP-------FIDNHDMPRFTVADGDTRNTDMALaVLLTSRGTPAV 389
Cdd:cd11359 289 dfpFNFYLLDLGANLSG-----NSINELVESWMSNMPegkwpnwVLGNHDNSRIASRLGPQYVRAMNM-LLLTLPGTPTT 362

                       410       420       430
                ....*....|....*....|....*....|....*
gi 62816022 390 YYGTE---------------QYLTGGNDPDnRKPM 409
Cdd:cd11359 363 YYGEEigmedvdisvdkekdPYTFESRDPE-RTPM 396
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 623-712 8.02e-26

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


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 102.35  E-value: 8.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 623 ATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWESGSNRQYTTPT 702
Cdd:cd05811  15 VTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIRKESDGSVTWESDPNRSYTVPS 94

                        90
                ....*....|..
gi 62816022 703 D--STGEYSGTW 712
Cdd:cd05811  95 GcgTTATVDDSW 106
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 50-394 8.85e-26

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 [Multi-domain]  Cd Length: 447  Bit Score: 111.12  E-value: 8.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  50 DDVIYQLISDRFRDGNPNNNptgelasddcsnlrkycgGDWQGIIDKIqsGYLTDLGVSAVWISP----PFENitavdsd 125
Cdd:cd11334   4 NAVIYQLDVRTFMDSNGDGI------------------GDFRGLTEKL--DYLQWLGVTAIWLLPfypsPLRD------- 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 126 igtsyHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGS-----YVaaYND 200
Cdd:cd11334  57 -----DGYDIADYYGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTS---DQHPWFQAARRDPDSpyrdyYV--WSD 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 201 DPKSYfhHNGGTDYSSYEDQIY-----RNLYNLADFDHHEAYID-------QYLKDAIKQWLDAGIDGIRVDAVAHM--- 265
Cdd:cd11334 127 TPPKY--KDARIIFPDVEKSNWtwdevAGAYYWHRFYSHQPDLNfdnpavrEEILRIMDFWLDLGVDGFRLDAVPYLier 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 266 ----------PPKWQKTLVDTIYDHRPvftfGEWFLG-ADQSNPRYYE-FSNDSGMSLL-DFRFGQEIRQVLRdfTDDWY 332
Cdd:cd11334 205 egtncenlpeTHDFLKRLRAFVDRRYP----DAILLAeANQWPEEVREyFGDGDELHMAfNFPLNPRLFLALA--REDAF 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 333 GFRDMLQETE--SEHDQvidQVPFIDNHD---------------MPRF------------------TVADGDTRNTDMAL 377
Cdd:cd11334 279 PIIDALRQTPpiPEGCQ---WANFLRNHDeltlemltdeerdyvYAAFapdprmriynrgirrrlaPMLGGDRRRIELAY 355

                       410
                ....*....|....*..
gi 62816022 378 AVLLTSRGTPAVYYGTE 394
Cdd:cd11334 356 SLLFSLPGTPVIYYGDE 372
AmyAc_OligoGlu_like cd11331
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 88-410 3.01e-24

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 [Multi-domain]  Cd Length: 450  Bit Score: 106.26  E-value: 3.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFENITAvdsDIGtsyhgYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:cd11331  25 GDLRGIISRLD--YLSDLGVDAVWLSPIYPSPMA---DFG-----YDVSDYCGIDPLFGTLEDFDRLVAEAHARGLKVIL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 168 DFVPNHTSP---------STSDGELEDGALYDNGSYVAAYNDDPKSYFhhnGGT--DYSSYEDQIYRNLY-------NLA 229
Cdd:cd11331  95 DFVPNHTSDqhpwflesrSSRDNPKRDWYIWRDPAPDGGPPNNWRSEF---GGSawTWDERTGQYYLHAFlpeqpdlNWR 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 230 DFDHHEAyidqyLKDAIKQWLDAGIDGIRVDAVAHM---------P--PKWQKtLVDTIYDHRPVFTfgewflgADQsnP 298
Cdd:cd11331 172 NPEVRAA-----MHDVLRFWLDRGVDGFRVDVLWLLikdpqfrdnPpnPDWRG-GMPPHERLLHIYT-------ADQ--P 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 299 RYYEFSndsgmslldfrfgQEIRQVLrdftdDWYGFRDMLQETESEHDQVID---------QVPF--------------- 354
Cdd:cd11331 237 ETHEIV-------------REMRRVV-----DEFGDRVLIGEIYLPLDRLVAyygagrdglHLPFnfhlislpwdaaala 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 355 -------------------IDNHDMPRFTVADGDTRnTDMALAVLLTSRGTPAVYYGTE--------------------- 394
Cdd:cd11331 299 raieeyeaalpagawpnwvLGNHDQPRIASRVGPAQ-ARVAAMLLLTLRGTPTLYYGDElgmedvpippervqdpaelnq 377

                       410
                ....*....|....*.
gi 62816022 395 QYLTGGNDPDnRKPMP 410
Cdd:cd11331 378 PGGGLGRDPE-RTPMP 392
AmyAc_maltase cd11328
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ...
 88-265 5.85e-24

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 [Multi-domain]  Cd Length: 470  Bit Score: 105.78  E-value: 5.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFENiTAVDSdigtsyhGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:cd11328  27 GDLKGITEKLD--YFKDIGIDAIWLSPIFKS-PMVDF-------GYDISDFTDIDPIFGTMEDFEELIAEAKKLGLKVIL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 168 DFVPNHTSPS--------TSDGELEDGALYDNGSYVAAYNDDP----KSYFHHNGGTdYSSYEDQIYRN--LYNLADFDH 233
Cdd:cd11328  97 DFVPNHSSDEhewfqksvKRDEPYKDYYVWHDGKNNDNGTRVPpnnwLSVFGGSAWT-WNEERQQYYLHqfAVKQPDLNY 175

                       170       180       190
                ....*....|....*....|....*....|..
gi 62816022 234 HEAYIDQYLKDAIKQWLDAGIDGIRVDAVAHM 265
Cdd:cd11328 176 RNPKVVEEMKNVLRFWLDKGVDGFRIDAVPHL 207
AmyAc_OligoGlu cd11330
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 52-403 6.81e-24

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 [Multi-domain]  Cd Length: 472  Bit Score: 105.81  E-value: 6.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRFRDGNPNnnptGElasddcsnlrkycgGDWQGIIDKIQsgYLTDLGVSAVWISPPFeniTAVDSDIGtsyh 131
Cdd:cd11330   7 VIYQIYPRSFLDSNGD----GI--------------GDLPGITEKLD--YIASLGVDAIWLSPFF---KSPMKDFG---- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 132 gYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpSTSDGELEDGALYDNGS---YVAAyndDPK----- 203
Cdd:cd11330  60 -YDVSDYCAVDPLFGTLDDFDRLVARAHALGLKVMIDQVLSHTS-DQHPWFEESRQSRDNPKadwYVWA---DPKpdgsp 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 204 -----SYFhhnGGT--DYSSYEDQIYrnLYNL----ADFDHHEAYIDQYLKDAIKQWLDAGIDGIRVDAV---AHMPpkw 269
Cdd:cd11330 135 pnnwlSVF---GGSawQWDPRRGQYY--LHNFlpsqPDLNFHNPEVQDALLDVARFWLDRGVDGFRLDAVnfyMHDP--- 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 270 qktlvdTIYDHRPVFTfGEWFLGADQSNPrYYEFSNDSGMSLLD-FRFGQEIRQVLRDFTDDW----------------- 331
Cdd:cd11330 207 ------ALRDNPPRPP-DEREDGVAPTNP-YGMQLHIHDKSQPEnLAFLERLRALLDEYPGRFlvgevsdddplevmaey 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 332 ----------YGF------------RDMLQETESEHDQVIDQVPFiDNHDMPR----FTVADGDTRNTDMALAVLLTSRG 385
Cdd:cd11330 279 tsggdrlhmaYSFdllgrpfsaavvRDALEAFEAEAPDGWPCWAF-SNHDVPRavsrWAGGADDPALARLLLALLLSLRG 357

                       410
                ....*....|....*...
gi 62816022 386 TPAVYYGTEQYLTGGNDP 403
Cdd:cd11330 358 SVCLYQGEELGLPEAELP 375
CBM_2 smart01065
Starch binding domain;
614-702 4.36e-23

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 93.57  E-value: 4.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022    614 ISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVGpfFNQVVHEYPNWYYDVNLP-AGTDIEFKFVKIASDGTVTWES 692
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVP--LSPDTDGYPLWKGTVSLPpAGTTIEYKYVKVDEDGSVTWES 78

                           90
                   ....*....|
gi 62816022    693 GSNRQYTTPT 702
Cdd:smart01065  79 GPNRRLTVPE 88
AmyAc_euk_bac_CMD_like cd11353
Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ...
 101-433 5.53e-22

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


Pssm-ID: 200490 [Multi-domain]  Cd Length: 366  Bit Score: 98.40  E-value: 5.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFEnitavdsdigTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTspstsd 180
Cdd:cd11353  38 HLKKLGINAIYFGPVFE----------SDSHGYDTRDYYKIDRRLGTNEDFKAVCKKLHENGIKVVLDGVFNHV------ 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 181 geledG----ALYD---NGsyvaaYNDDPKSYFH------HNGGTDYSSYEDqiYRNLYNLADFDHHEAYIDQYLKDAIK 247
Cdd:cd11353 102 -----GrdffAFKDvqeNR-----ENSPYKDWFKgvnfdgNSPYNDGFSYEG--WEGHYELVKLNLHNPEVVDYLFDAVR 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 248 QWLDA-GIDGIRVDAVAHMPPKWQKTLVDTIYDHRPVFtfgeWFLG----ADqsnprYYEFSND---------------- 306
Cdd:cd11353 170 FWIEEfDIDGLRLDVADCLDFDFLRELRDFCKSLKPDF----WLMGevihGD-----YNRWANDemldsvtnyecykgly 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 307 SGMSLLDFrFgqEIRQVL-RDFTDD-WYGFRDMLQetesehdqvidqvpFIDNHDMPRFTVADGDTRNTDMALAVLLTSR 384
Cdd:cd11353 241 SSHNDHNY-F--EIAHSLnRQFGLEgIYRGKHLYN--------------FVDNHDVNRIASILKNKEHLPPIYALLFTMP 303

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62816022 385 GTPAVYYGTEQYLTG----GNDPDNRKPMPSFDTTT-----TAYkvIQALTSLRSSNR 433
Cdd:cd11353 304 GIPSIYYGSEWGIEGvkgnGSDAALRPALDEPELSGennelTDL--IAKLARIRRASP 359
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 89-390 1.78e-20

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


Pssm-ID: 200454 [Multi-domain]  Cd Length: 352  Bit Score: 93.50  E-value: 1.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  89 DW--QGIIDKIQSgyLTDLGVSAVWISPPFENITAVDSDiGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVV 166
Cdd:cd11315   9 DWsfNTIKENLPE--IAAAGYTAIQTSPPQKSKEGGNEG-GNWWYRYQPTDYRIGNNQLGTEDDFKALCAAAHKYGIKII 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 167 IDFVPNHTspsTSDGELEDGALYDNgsyVAAYNDDPKSYFHHNGGTDYSSYEDQIYRNLYNLADFDHHEAYIDQYLKDAI 246
Cdd:cd11315  86 VDVVFNHM---ANEGSAIEDLWYPS---ADIELFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKAYL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 247 KQWLDAGIDGIRVDAVAHMP----PKWQKTLVDTI---YDHRPVFTFGEwFLGADQSNPRYYEfSNDSGMSLLDFRFGQE 319
Cdd:cd11315 160 KALVALGVDGFRFDAAKHIElpdePSKASDFWTNIlnnLDKDGLFIYGE-VLQDGGSRDSDYA-SYLSLGGVTASAYGFP 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 320 IRQVLR-------DFTDDWYGfrDMLQETESehdqvidqVPFIDNHDmprfTVADGDTRNT-----DMALA-VLLTSR-- 384
Cdd:cd11315 238 LRGALKnaflfggSLDPASYG--QALPSDRA--------VTWVESHD----TYNNDGFESTglddeDERLAwAYLAARdg 303


                ....*.
gi 62816022 385 GTPAVY 390
Cdd:cd11315 304 GTPLFF 309
CBM20_beta_amylase cd05809
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ...
 618-712 1.13e-19

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: 84.60  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 618 FVVNDATTDVGENVYVVGNVHELGDWDTDRAVGPFFNQvvHEYPNWYYDVNLPAGTDIEFKFVKIASDGT-VTWESGSNR 696
Cdd:cd05809   7 FVVKNVPTTIGETVYITGSRAELGNWDTKQYPIQLYYN--SHSNDWRGTVHLPAGRNIEFKAIKKSKDGTnKSWQGGQQS 84

                        90
                ....*....|....*.
gi 62816022 697 QYTTPTdSTGEYSGTW 712
Cdd:cd05809  85 WYPVPL-GTTSYTSSW 99
AmyAc_OligoGlu_TS cd11332
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ...
 50-265 3.00e-19

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 [Multi-domain]  Cd Length: 481  Bit Score: 91.57  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  50 DDVIYQLISDRFRDGNPNNNptgelasddcsnlrkycgGDWQGIIDKIqsGYLTDLGVSAVWISPPFENITAvdsDigts 129
Cdd:cd11332   5 DAVVYQVYPRSFADANGDGI------------------GDLAGIRARL--PYLAALGVDAIWLSPFYPSPMA---D---- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 130 yHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTS-------------PSTS--------DGELEDGAL 188
Cdd:cd11332  58 -GGYDVADYRDVDPLFGTLADFDALVAAAHELGLRVIVDIVPNHTSdqhpwfqaalaagPGSPeraryifrDGRGPDGEL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 189 YDNgsyvaayndDPKSYFhhnGG------TDYSSYEDQIYRNLYNLA--DFDHHEAYIDQYLKDAIKQWLDAGIDGIRVD 260
Cdd:cd11332 137 PPN---------NWQSVF---GGpawtrvTEPDGTDGQWYLHLFAPEqpDLNWDNPEVRAEFEDVLRFWLDRGVDGFRID 204


                ....*
gi 62816022 261 aVAHM 265
Cdd:cd11332 205 -VAHG 208
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 88-394 2.25e-18

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 [Multi-domain]  Cd Length: 390  Bit Score: 87.71  E-value: 2.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIqsGYLTDLGVSAVWISPpfenITAVDSDIGTSYH--GYWArdftdPNEFFGDMETFKQLVDVAHQNGIKV 165
Cdd:cd11350  30 GDFKGVIDKL--DYLQDLGVNAIELMP----VQEFPGNDSWGYNprHYFA-----LDKAYGTPEDLKRLVDECHQRGIAV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 166 VIDFVPNHT---SPSTSdgeledgaLYDNGsyvaAYNDDPKSYFHHNGGTDYSSYEDQiyrnlynlaDFDHHEAYIDQYL 242
Cdd:cd11350  99 ILDVVYNHAegqSPLAR--------LYWDY----WYNPPPADPPWFNVWGPHFYYVGY---------DFNHESPPTRDFV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 243 KDAIKQWLDA-GIDGIRVDAVAHMppkWQK-TLVDTIYDHRP-VFTFGEWFL-GADQSNPRYY-------------EFSN 305
Cdd:cd11350 158 DDVNRYWLEEyHIDGFRFDLTKGF---TQKpTGGGAWGGYDAaRIDFLKRYAdEAKAVDKDFYviaehlpdnpeetELAT 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 306 DSGM----SLLDFRF---GQEIRQVLRDFTDDWYGFRDMLQETesehdqvidQVPFIDNHDMPRFTVADGDTRNTD---- 374
Cdd:cd11350 235 YGMSlwgnSNYSFSQaamGYQGGSLLLDYSGDPYQNGGWSPKN---------AVNYMESHDEERLMYKLGAYGNGNsylg 305

                       330       340       350
                ....*....|....*....|....*....|.
gi 62816022 375 -----------MALAVLLTSRGTPAVYYGTE 394
Cdd:cd11350 306 inletalkrlkLAAAFLFTAPGPPMIWQGGE 336
AmyAc_2 cd11348
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 88-409 3.24e-17

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 [Multi-domain]  Cd Length: 429  Bit Score: 84.67  E-value: 3.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIQsgYLTDLGVSAVWISPPFenitavDSDIGTSyhGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:cd11348  19 GDLQGIISKLD--YIKSLGCNAIWLNPCF------DSPFKDA--GYDVRDYYKVAPRYGTNEDLVRLFDEAHKRGIHVLL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 168 DFVPNHTS-------PSTSDGELEDGALY----------DNGSYVAAYNDDPKSYFhhnggTDYssYEDQIYRNlYNLAD 230
Cdd:cd11348  89 DLVPGHTSdehpwfkESKKAENNEYSDRYiwtdsiwsggPGLPFVGGEAERNGNYI-----VNF--FSCQPALN-YGFAH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 231 FDHHE---AYID-------QYLKDAIKQWLDAGIDGIRVDA----VAHMPPK------WQKtLVDTIYDHRPVFTF-GEW 289
Cdd:cd11348 161 PPTEPwqqPVDApgpqatrEAMKDIMRFWLDKGADGFRVDMadslVKNDPGNketiklWQE-IRAWLDEEYPEAVLvSEW 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 290 flgadqSNPRYyefSNDSGMSLldfrfgqeirqvlrDFTDDWYG------FRDMLQETESEHDQ-VIDQV------PFID 356
Cdd:cd11348 240 ------GNPEQ---SLKAGFDM--------------DFLLHFGGngynslFRNLNTDGGHRRDNcYFDASgkgdikPFVD 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 357 --------------------NHDMPRFTvadgdTRNTD----MALAVLLTSRGTPAVYYGTE---QYLT-------GGND 402
Cdd:cd11348 297 eylpqyeatkgkgyislptcNHDTPRLN-----ARLTEeelkLAFAFLLTMPGVPFIYYGDEigmRYIEglpskegGYNR 371


                ....*..
gi 62816022 403 PDNRKPM 409
Cdd:cd11348 372 TGSRTPM 378
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
81-410 1.08e-15

bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 81.47  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022    81 NLRkycgGDWQGIIDKIQSGYLTDLGVSAVWISPPFENITA--VDSDIGTSYHGYWARDFTDPNEFFG--DMETFKQLVD 156
Cdd:PRK14510  179 NLR----GTFAKLAAPEAISYLKKLGVSIVELNPIFASVDEhhLPQLGLSNYWGYNTVAFLAPDPRLApgGEEEFAQAIK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   157 VAHQNGIKVVIDFVPNHTSpstSDGELedgalydnGSYVAAYNDDPKSYFHHNGGTDySSYEDQI-YRNLYNLadfdhHE 235
Cdd:PRK14510  255 EAQSAGIAVILDVVFNHTG---ESNHY--------GPTLSAYGSDNSPYYRLEPGNP-KEYENWWgCGNLPNL-----ER 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   236 AYIDQYLKDAIKQWLDAGIDGIRVD---AVAHMPpkwqktlvDTIYD-HRPvftfgewFLGADQSNPRYYEFSN------ 305
Cdd:PRK14510  318 PFILRLPMDVLRSWAKRGVDGFRLDladELAREP--------DGFIDeFRQ-------FLKAMDQDPVLRRLKMiaevwd 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   306 --DSGMSLLDFR--FGQ---EIRQVLRDFtddWYGFRDMLQETES-----------EHDQVIDQVPFIDNHDmpRFTVAD 367
Cdd:PRK14510  383 dgLGGYQYGKFPqyWGEwndPLRDIMRRF---WLGDIGMAGELATrlagsadifphRRRNFSRSINFITAHD--GFTLLD 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   368 --------------GDTRNTD---------------------------MALAVLLTSRGTPAVYYGTE--QYLTGGN--- 401
Cdd:PRK14510  458 lvsfnhkhneangeDNRDGTPdnqswncgvegytldaairslrrrrlrLLLLTLMSFPGVPMLYYGDEagRSQNGNNngy 537

                         410
                  ....*....|
gi 62816022   402 -DPDNRKPMP 410
Cdd:PRK14510  538 aQDNNRGTYP 547
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 614-712 4.79e-15

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: 71.29  E-value: 4.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 614 ISARFVVNDATTDVGENVYVVGNVHELGDWDTDRAVgpffNQVVHEYPNWYYDVNLPAGTDIEFKFVK-IASDGT--VTW 690
Cdd:cd05810   1 VSVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAV----KLDPTAYPTWSGSISLPASTNVEWKCLKrNETNPTagVQW 76

                        90       100
                ....*....|....*....|..
gi 62816022 691 ESGSNRQYTTPtDSTGEYSGTW 712
Cdd:cd05810  77 QGGGNNQLTTG-NSTASTSGSF 97
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 90-392 4.93e-15

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 78.39  E-value: 4.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   90 WQGIIDKIQSgyLTDLGVSAVWISPPFEnitavdSDIGTSYHGYWARDFTDPNEF---------FGDMETFKQLVDVAHQ 160
Cdd:PRK09441  21 WNRLAERAPE--LAEAGITAVWLPPAYK------GTSGGYDVGYGVYDLFDLGEFdqkgtvrtkYGTKEELLNAIDALHE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  161 NGIKVVIDFVPNHTS------------PSTSDGELEDGALYDNGSYV--------AAYNDDPKSYFHHNGgTDYSSYEDQ 220
Cdd:PRK09441  93 NGIKVYADVVLNHKAgadeketfrvveVDPDDRTQIISEPYEIEGWTrftfpgrgGKYSDFKWHWYHFSG-TDYDENPDE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  221 --IYRNL---------------------YNLADFDHHEAYID-----QYLKDAIkqwldaGIDGIRVDAVAHMPPKWQKT 272
Cdd:PRK09441 172 sgIFKIVgdgkgwddqvddengnfdylmGADIDFRHPEVREElkywaKWYMETT------GFDGFRLDAVKHIDAWFIKE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  273 LVDTIYDH--RPVFTFGEWFLGaDQSNPRYYEFSNDSGMSLLDFR---FGQEIRQVLRDFtDDWYGFRDMLQETESEHdq 347
Cdd:PRK09441 246 WIEHVREVagKDLFIVGEYWSH-DVDKLQDYLEQVEGKTDLFDVPlhyNFHEASKQGRDY-DMRNIFDGTLVEADPFH-- 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 62816022  348 vidQVPFIDNHDMPRFTVADG--DTRNTDMALAVLLT-SRGTPAVYYG 392
Cdd:PRK09441 322 ---AVTFVDNHDTQPGQALESpvEPWFKPLAYALILLrEEGYPCVFYG 366
PRK10933 PRK10933
trehalose-6-phosphate hydrolase; Provisional
 52-303 2.19e-14

trehalose-6-phosphate hydrolase; Provisional


Pssm-ID: 182849 [Multi-domain]  Cd Length: 551  Bit Score: 76.33  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   52 VIYQLISDRFRDGNPNNNptgelasddcsnlrkycgGDWQGIIDKIQsgYLTDLGVSAVWISPpFENITAVDSdigtsyh 131
Cdd:PRK10933  12 VIYQIYPKSFQDTTGSGT------------------GDLRGVTQRLD--YLQKLGVDAIWLTP-FYVSPQVDN------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  132 GYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSpstSDGELEDGALYDNGSYVAAY-----NDD--PKS 204
Cdd:PRK10933  64 GYDVANYTAIDPTYGTLDDFDELVAQAKSRGIRIILDMVFNHTS---TQHAWFREALNKESPYRQFYiwrdgEPEtpPNN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  205 YFHHNGGTDYSSYED--QIYRNLY--NLADFD-HHEAYIDQyLKDAIKQWLDAGIDGIRVDaVAHMPPKWQKTLVDTIYD 279
Cdd:PRK10933 141 WRSKFGGSAWRWHAEseQYYLHLFapEQADLNwENPAVRAE-LKKVCEFWADRGVDGLRLD-VVNLISKDQDFPDDLDGD 218

                        250       260
                 ....*....|....*....|....
gi 62816022  280 HRPVFTFGewflgadqsnPRYYEF 303
Cdd:PRK10933 219 GRRFYTDG----------PRAHEF 232
AmyAc_GTHase cd11325
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ...
 87-394 4.59e-14

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 [Multi-domain]  Cd Length: 436  Bit Score: 74.89  E-value: 4.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  87 GGDWQGIIDKIqsGYLTDLGVSAVWISPpfenITAVDSDIGTSYHG--YWArdftdPNEFFGDMETFKQLVDVAHQNGIK 164
Cdd:cd11325  51 EGTFDAAIERL--DYLADLGVTAIELMP----VAEFPGERNWGYDGvlPFA-----PESSYGGPDDLKRLVDAAHRRGLA 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 165 VVIDFVPNHTSPStsdgeledgalydnGSYVAAYNDDpksYFHHNGGTDYSsyeDQIyrnlynlaDFDHHEAYIDQYLKD 244
Cdd:cd11325 120 VILDVVYNHFGPD--------------GNYLWQFAGP---YFTDDYSTPWG---DAI--------NFDGPGDEVRQFFID 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 245 AIKQWL-DAGIDGIRVDAVAHM----PPKWQKTLVDTI---YDHRPVFTFGEwflgADQSNPRYYEFSNDSGMSL----- 311
Cdd:cd11325 172 NALYWLrEYHVDGLRLDAVHAIrddsGWHFLQELAREVraaAAGRPAHLIAE----DDRNDPRLVRPPELGGAGFdaqwn 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 312 -------------------LDFRFGQEIRQVLRD---FTDDWYGFRDMLQETESEHDQVIDQVPFIDNHDM--------- 360
Cdd:cd11325 248 ddfhhalhvaltgeregyyADFGPAEDLARALAEgfvYQGQYSPFRGRRHGRPSADLPPTRFVVFLQNHDQvgnraager 327

                       330       340       350
                ....*....|....*....|....*....|....
gi 62816022 361 PRFTVADGDTRntdMALAVLLTSRGTPAVYYGTE 394
Cdd:cd11325 328 LSSLAAPARLR---LAAALLLLSPGIPMLFMGEE 358
Aamy_C smart00632
Aamy_C domain;
441-514 5.16e-14

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 67.65  E-value: 5.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62816022    441 EERWINSD-VFVYERefgDNVVLVAINRSlDWYDVSGLQTSLPEGTYDDALGGTLDGFSTTVNTDGsIDTFSVGP 514
Cdd:smart00632   1 TNWWDNGDnQIAFER---GSKGFVAINRS-DSDLTITLQTSLPAGTYCDVISGLCTGKSVTVGSNG-IATFTLPA 70
GlgB COG0296
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism];
87-265 1.09e-12

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


Pssm-ID: 440065 [Multi-domain]  Cd Length: 625  Bit Score: 71.32  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  87 GGDWQGIIDKIQSgYLTDLGVSAVWISP----PFE-----NITavdsdigtsyhGYWArdftdPNEFFGDMETFKQLVDV 157
Cdd:COG0296 162 FLTYRELAERLVP-YLKELGFTHIELMPvaehPFDgswgyQPT-----------GYFA-----PTSRYGTPDDFKYFVDA 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 158 AHQNGIKVVIDFVPNHTSPstsDGE-LE--DG-ALYdngsyvaaYNDDPKSYFHhnggTDYSSYedqIYrnlynlaDFDH 233
Cdd:COG0296 225 CHQAGIGVILDWVPNHFPP---DGHgLArfDGtALY--------EHADPRRGEH----TDWGTL---IF-------NYGR 279

                       170       180       190
                ....*....|....*....|....*....|...
gi 62816022 234 HEayIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:COG0296 280 NE--VRNFLISNALYWLEEfHIDGLRVDAVASM 310
AmyAc_Glg_BE cd11322
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ...
 132-265 4.02e-12

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


Pssm-ID: 200461 [Multi-domain]  Cd Length: 402  Bit Score: 68.70  E-value: 4.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 132 GYWArdftdPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPstsdgelEDGALYdngsyvaaynddpksYFhhNGG 211
Cdd:cd11322  96 GYFA-----PTSRYGTPDDFKYFVDACHQAGIGVILDWVPGHFPK-------DDHGLA---------------RF--DGT 146

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 212 TDY-SSYEDQIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:cd11322 147 PLYeYPDPRKGEHPDWGTLNFDYGRNEVRSFLISNALYWLEEyHIDGLRVDAVSSM 202
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 101-392 3.17e-11

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


Pssm-ID: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 65.62  E-value: 3.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFEnitAVDSDIGTsyhGYWARDFTDPNEF---------FGDMETFKQLVDVAHQNGIKVVIDFVP 171
Cdd:cd11318  28 ELAELGITAVWLPPAYK---GASGTEDV---GYDVYDLYDLGEFdqkgtvrtkYGTKEELLEAIKALHENGIQVYADAVL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 172 NH------------TSPSTSDGELEDGALYDNGSYVA--------AYNDDpKSYFHHNGGTDYSSYEDQ--IYRNLYNL- 228
Cdd:cd11318 102 NHkagadetetvkaVEVDPNDRNKEISEPYEIEAWTKftfpgrggKYSDF-KWNWQHFSGVDYDQKTKKkgIFKINFEGk 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 229 ------------------ADFDH-HEAYIDQyLKDAIKqWL--DAGIDGIRVDAVAHMPPKWQKTLVDTIYDH--RPVFT 285
Cdd:cd11318 181 gwdedvddengnydylmgADIDYsNPEVREE-LKRWGK-WYinTTGLDGFRLDAVKHISASFIKDWIDHLRREtgKDLFA 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 286 FGEWFLGADQSNPRYYEFSNDSgMSLLD----FRFGQEIRQV----LRDFtddwygFRDMLQETESEHdqvidQVPFIDN 357
Cdd:cd11318 259 VGEYWSGDLEALEDYLDATDGK-MSLFDvplhYNFHEASKSGgnydLRKI------FDGTLVQSRPDK-----AVTFVDN 326

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 62816022 358 HDM-----------PRFtvadgdtrntdMALA---VLLTSRGTPAVYYG 392
Cdd:cd11318 327 HDTqpgqsleswvePWF-----------KPLAyalILLRKDGYPCVFYG 364
AmyAc_3 cd11349
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 52-267 2.11e-10

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 [Multi-domain]  Cd Length: 456  Bit Score: 63.46  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  52 VIYQLISDRFRDGNPNNNPTGELASDDCsnlrkycgGDWQGIIDKIQSgYLTDLGVSAVWISPPFE----------NITA 121
Cdd:cd11349   2 IIYQLLPRLFGNKNTTNIPNGTIEENGV--------GKFNDFDDTALK-EIKSLGFTHVWYTGVIRhatqtdysayGIPP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 122 VDSDI--GTSYHGYWARDF--------TDPNeffGDMETFKQLVDVAHQNGIKVVIDFVPNHT-----SPSTSDGELEDG 186
Cdd:cd11349  73 DDPDIvkGRAGSPYAIKDYydvdpdlaTDPT---NRMEEFEALVERTHAAGLKVIIDFVPNHVarqyhSDAKPEGVKDFG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 187 ALYDNGSYVAAYND-------------------DPKSYFHH-------NGGTDYSSYEDQIYRNL---YN---LADFDHH 234
Cdd:cd11349 150 ANDDTSKAFDPSNNfyylpgepfvlpfslngspATDGPYHEspakatgNDCFSAAPSINDWYETVklnYGvdyDGGGSFH 229

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62816022 235 EAYI-DQYLK-DAIKQ-WLDAGIDGIRVDaVAHMPP 267
Cdd:cd11349 230 FDPIpDTWIKmLDILLfWAAKGVDGFRCD-MAEMVP 264
PRK12313 PRK12313
1,4-alpha-glucan branching protein GlgB;
132-265 4.18e-10

1,4-alpha-glucan branching protein GlgB;


Pssm-ID: 237052 [Multi-domain]  Cd Length: 633  Bit Score: 63.00  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  132 GYWARDFTdpnefFGDMETFKQLVDVAHQNGIKVVIDFVPNHTspsTSDGeleDGALYDNGSYVAAYnDDPKSYFHHNGG 211
Cdd:PRK12313 208 GYFAPTSR-----YGTPEDFMYLVDALHQNGIGVILDWVPGHF---PKDD---DGLAYFDGTPLYEY-QDPRRAENPDWG 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62816022  212 TdyssyedqiyrnlYNladFDHHEAYIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:PRK12313 276 A-------------LN---FDLGKNEVRSFLISSALFWLDEyHLDGLRVDAVSNM 314
AmyAc_MTSase cd11336
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ...
 101-173 5.57e-10

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 [Multi-domain]  Cd Length: 660  Bit Score: 62.51  E-value: 5.57e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 101 YLTDLGVSAVWISPPFeniTAVDSdigtSYHGYwarDFTDP---NEFFGDMETFKQLVDVAHQNGIKVVIDFVPNH 173
Cdd:cd11336  22 YLADLGISHLYASPIL---TARPG----STHGY---DVVDHtriNPELGGEEGLRRLAAALRAHGMGLILDIVPNH 87
PLN02784 PLN02784
alpha-amylase
 102-290 7.28e-10

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 62.34  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  102 LTDLGVSAVWISPPFENItavdsdigtSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSP--STS 179
Cdd:PLN02784 530 LSSLGFTVVWLPPPTESV---------SPEGYMPKDLYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRCAhfQNQ 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  180 DG--ELEDGAL-YDNGSYVAaynDDPksyfHHNGGTDYSSYEdqiyrNLYNLADFDHHEAYIdqylKDAIKQWL-----D 251
Cdd:PLN02784 601 NGvwNIFGGRLnWDDRAVVA---DDP----HFQGRGNKSSGD-----NFHAAPNIDHSQDFV----RKDLKEWLcwmrkE 664

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 62816022  252 AGIDGIRVDAVAHMppkWQKTLVDTIYDHRPVFTFGEWF 290
Cdd:PLN02784 665 VGYDGWRLDFVRGF---WGGYVKDYMEASEPYFAVGEYW 700
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 102-391 7.36e-10

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


Pssm-ID: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 60.70  E-value: 7.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 102 LTDLGVSAVWISPPFEnitavdsDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPstsdg 181
Cdd:cd11314  27 LAAAGFTAIWLPPPSK-------SVSGSSMGYDPGDLYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSG----- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 182 eledgalYDNG-SYVAAYNDDpksyfHHNggtdyssyeDQIYRNLYNLADfdhheayidqYLKDaikqwlDAGIDGIRVD 260
Cdd:cd11314  95 -------PDTGeDFGGAPDLD-----HTN---------PEVQNDLKAWLN----------WLKN------DIGFDGWRFD 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 261 AVAHMPPKWQKTLVDTIydhRPVFTFGEWFLGADQSNP-----RYYEFSNDSGM--SLLDFRFgqeiRQVLRD-FTDDWY 332
Cdd:cd11314 138 FVKGYAPSYVKEYNEAT---SPSFSVGEYWDGLSYENQdahrqRLVDWIDATGGgsAAFDFTT----KYILQEaVNNNEY 210

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62816022 333 GFRDMLQETESEHDQVIDQ--VPFIDNHDM-PRFTVADGDTRNTDMALAVLLTSRGTPAVYY 391
Cdd:cd11314 211 WRLRDGQGKPPGLIGWWPQkaVTFVDNHDTgSTQGHWPFPTDNVLQGYAYILTHPGTPCVFW 272
TreY COG3280
Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];
101-173 7.76e-10

Maltooligosyltrehalose synthase [Carbohydrate transport and metabolism];


Pssm-ID: 442511 [Multi-domain]  Cd Length: 915  Bit Score: 62.52  E-value: 7.76e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022 101 YLTDLGVSAVWISPPFeniTAVdsdIGtSYHGYwarDFTDPNEF---FGDMETFKQLVDVAHQNGIKVVIDFVPNH 173
Cdd:COG3280  27 YLARLGISHLYASPIL---KAR---PG-STHGY---DVVDHNRInpeLGGEEGFERLVAALRAHGMGLILDIVPNH 92
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 625-703 1.43e-09

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


Pssm-ID: 99890  Cd Length: 99  Bit Score: 55.80  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 625 TDVGEN--VYVVGNVHELGDWDTDRAVgpffNQVVHEYPNWYYDVNLPAGT-DIEFKFVKI-ASDGTVTWESGSNRQYTT 700
Cdd:cd05816   9 PYVPKGqsVYVTGSSPELGNWDPQKAL----KLSDVGFPIWEADIDISKDSfPFEYKYIIAnKDSGVVSWENGPNRELSA 84


                ...
gi 62816022 701 PTD 703
Cdd:cd05816  85 PSL 87
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 628-712 2.25e-09

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99892  Cd Length: 92  Bit Score: 54.82  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 628 GENVYVVGNVHELGDWDtdravgpffNQVVHEYPN--WYYDVNLPAGTDIEFKFVKIASDGTVTWESGSNRQYTTPTDST 705
Cdd:cd05818  15 GEHVAILGSTKELGSWK---------KKVPMNWTEngWVCDLELDGGELVEYKFVIVKRDGSVIWEGGNNRVLELPKEGN 85


                ....*..
gi 62816022 706 GEYSGTW 712
Cdd:cd05818  86 FEIVCHW 92
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 106-390 3.15e-09

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 59.11  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 106 GVSAVWISPPFENITAVDSDIGTSYHgywardftdP-----NEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTspsTSD 180
Cdd:cd11317  27 GYGGVQVSPPQEHIVGPGRPWWERYQ---------PvsyklNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHM---AGD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 181 GEledgalydngsyvaaynddpksyfhhnggtdyssyedqIYRN--LYNLADFDHHEAYIDQYLKDAIKQWLDAGIDGIR 258
Cdd:cd11317  95 AN--------------------------------------EVRNceLVGLADLNTESDYVRDKIADYLNDLISLGVAGFR 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 259 VDAVAHMPP-------KWQKTLVDTIYDHRPvFTFGEWFLGADQS-NPRYYEFSNDsgmsLLDFRFGQEIRQVLRDFTDD 330
Cdd:cd11317 137 IDAAKHMWPedlaailARLKDLNGGPLGSRP-YIYQEVIDGGGEAiQPSEYTGNGD----VTEFRYARGLSNAFRGKIKL 211

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62816022 331 WY----GFRDMLqeTESEHDQVidqvpFIDNHDMPRFTVADGDT------RNTDMALAVLLTSR-GTPAVY 390
Cdd:cd11317 212 LLlknfGEGWGL--LPSERAVV-----FVDNHDNQRGHGGGGDMltykdgRRYKLANAFMLAWPyGTPRVM 275
trehalose_TreY TIGR02401
malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan ...
 101-173 3.27e-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 [Multi-domain]  Cd Length: 825  Bit Score: 60.11  E-value: 3.27e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62816022   101 YLTDLGVSAVWISPPFeniTAVdsdiGTSYHGYwarDFTDPNEF---FGDMETFKQLVDVAHQNGIKVVIDFVPNH 173
Cdd:TIGR02401  24 YLKSLGVSHLYLSPIL---TAV----PGSTHGY---DVVDHSEInpeLGGEEGLRRLSEAARARGLGLIVDIVPNH 89
AmyAc_Amylosucrase cd11324
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ...
 87-175 4.19e-09

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: 59.51  E-value: 4.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  87 GGDWQGIIDKIQsgYLTDLGVSAVWISPPFenitavDSDIGTSYHGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVV 166
Cdd:cd11324  82 AGDLKGLAEKIP--YLKELGVTYLHLMPLL------KPPEGDNDGGYAVSDYREVDPRLGTMEDLRALAAELRERGISLV 153


                ....*....
gi 62816022 167 IDFVPNHTS 175
Cdd:cd11324 154 LDFVLNHTA 162
PRK05402 PRK05402
1,4-alpha-glucan branching protein GlgB;
145-265 5.91e-09

1,4-alpha-glucan branching protein GlgB;


Pssm-ID: 235445 [Multi-domain]  Cd Length: 726  Bit Score: 59.42  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  145 FGDMETFKQLVDVAHQNGIKVVIDFVPNHTsPSTS------DGEledgALYDNGsyvaayndDPKSYFHHNGGTdyssye 218
Cdd:PRK05402 311 FGTPDDFRYFVDACHQAGIGVILDWVPAHF-PKDAhglarfDGT----ALYEHA--------DPREGEHPDWGT------ 371

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 62816022  219 dQIYrnlynlaDFDHHEayIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:PRK05402 372 -LIF-------NYGRNE--VRNFLVANALYWLEEfHIDGLRVDAVASM 409
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 101-466 9.96e-09

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 [Multi-domain]  Cd Length: 477  Bit Score: 58.16  E-value: 9.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFENitavdsdigtsyhgywardfTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTS---PS 177
Cdd:cd11329  87 AISKLGAKGVIYELPADE--------------------TYLNNSYGVESDLKELVKTAKQKDIKVILDLTPNHSSkqhPL 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 178 TSDGELEDGALYDngSYV---AAYNDDPKSYFHHNGGTDYSSYED-QIYRNLYNLA--DFDHHEAYIDQYLKDAIKQWLD 251
Cdd:cd11329 147 FKDSVLKEPPYRS--AFVwadGKGHTPPNNWLSVTGGSAWKWVEDrQYYLHQFGPDqpDLNLNNPAVVDELKDVLKHWLD 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 252 AGIDGIRVDAVAHM----------PPKWQKTLVDTIYD---HR---------PVftFGEW-------------FLGADQS 296
Cdd:cd11329 225 LGVRGFRLANAKYLledpnlkdeeISSNTKGVTPNDYGfytHIkttnlpelgEL--LREWrsvvknytdggglSVAEDII 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 297 NPRYYEFSNDSGMsLLDFRFGQEIRQVLR-DFTDDWYGFRDMLQETESEHDQVIdQVPFIDNhDMPrftvadgdtRNTDM 375
Cdd:cd11329 303 RPDVYQVNGTLDL-LIDLPLYGNFLAKLSkAITANALHKILASISTVSATTSWP-QWNLRYR-DTK---------VVASD 370

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 376 ALAV---LLTsrGTPAVYYGTEqylTGGNDpdnrkpmpSFDTTTTaykviqaLTSLRSSNRRSPTADTEERWINSDVFVY 452
Cdd:cd11329 371 ALTLftsLLP--GTPVVPLDSE---LYANV--------SKPTIST-------LEKFRATPSIQHGSFNAYLLNNDTVFAY 430

                       410
                ....*....|....*
gi 62816022 453 ER-EFGDNVVLVAIN 466
Cdd:cd11329 431 TRiKSGNPGYLVALN 445
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 625-700 1.29e-08

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: 52.86  E-value: 1.29e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62816022 625 TDVGENVYVVGNVHELGDWDTDRAVGPFFNqvvhEYPNWYYDVNLPAGTDIEFKFV--KIASDGTVTWESGSNRQYTT 700
Cdd:cd05817  10 TQFGEAVYISGNCNQLGNWNPSKAKRMQWN----EGDLWTVDVGIPESVYIEYKYFvsNYDDPNTVLWESGPNRVLRT 83
PRK14511 PRK14511
malto-oligosyltrehalose synthase;
100-173 3.70e-08

malto-oligosyltrehalose synthase;


Pssm-ID: 237740 [Multi-domain]  Cd Length: 879  Bit Score: 56.91  E-value: 3.70e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62816022  100 GYLTDLGVSAVWISPPFeniTAVDSdigtSYHGYwarDFTDPNEF---FGDMETFKQLVDVAHQNGIKVVIDFVPNH 173
Cdd:PRK14511  27 PYFADLGVSHLYLSPIL---AARPG----STHGY---DVVDHTRInpeLGGEEGLRRLAAALRAHGMGLILDIVPNH 93
PRK14705 PRK14705
glycogen branching enzyme; Provisional
 101-265 1.53e-07

glycogen branching enzyme; Provisional


Pssm-ID: 237794 [Multi-domain]  Cd Length: 1224  Bit Score: 55.01  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   101 YLTDLGVSAVWISPPFENitavdsDIGTSYhGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNH-TSPSTS 179
Cdd:PRK14705  774 YVKWLGFTHVEFMPVAEH------PFGGSW-GYQVTSYFAPTSRFGHPDEFRFLVDSLHQAGIGVLLDWVPAHfPKDSWA 846

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   180 DGELEDGALYDNGsyvaayndDPKSYFHHNGGTdyssyedqiyrnlynlADFDHHEAYIDQYLKDAIKQWLDA-GIDGIR 258
Cdd:PRK14705  847 LAQFDGQPLYEHA--------DPALGEHPDWGT----------------LIFDFGRTEVRNFLVANALYWLDEfHIDGLR 902


                  ....*..
gi 62816022   259 VDAVAHM 265
Cdd:PRK14705  903 VDAVASM 909
PRK14706 PRK14706
glycogen branching enzyme; Provisional
 101-265 2.24e-07

glycogen branching enzyme; Provisional


Pssm-ID: 237795 [Multi-domain]  Cd Length: 639  Bit Score: 54.22  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  101 YLTDLGVSAVWISPPFENitAVDSDIGTSYHGYWArdftdPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTSD 180
Cdd:PRK14706 176 YVTYMGYTHVELLGVMEH--PFDGSWGYQVTGYYA-----PTSRLGTPEDFKYLVNHLHGLGIGVILDWVPGHFPTDESG 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  181 GELEDGA-LYDNGsyvaayndDPKSYFHHNggtdyssyedqiyrnlYNLADFDHHEAYIDQYLKDAIKQWL-DAGIDGIR 258
Cdd:PRK14706 249 LAHFDGGpLYEYA--------DPRKGYHYD----------------WNTYIFDYGRNEVVMFLIGSALKWLqDFHVDGLR 304


                 ....*..
gi 62816022  259 VDAVAHM 265
Cdd:PRK14706 305 VDAVASM 311
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 444-523 9.89e-07

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 47.33  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   444 WIN-----SDVFVYEREFGDNVVLVAINRS-LDWYdvSGLQTSLPE-GTYDDAL-------GGTLDGFSTTVNTDG--SI 507
Cdd:pfam02806   1 WIDgddaeNNVIAFERGDDGGKLLVVFNFTpSVSY--TDYRTGLPEaGTYCEVLntddeeyGGSNTGEVVTVDGPGhpNS 78

                          90
                  ....*....|....*.
gi 62816022   508 DTFSVGPQTVCVWEHT 523
Cdd:pfam02806  79 LTLTLPPLSALVLKVE 94
AmyAc_SLC3A2 cd11345
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ...
 88-271 1.76e-06

Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. 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: 200483 [Multi-domain]  Cd Length: 326  Bit Score: 50.52  E-value: 1.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  88 GDWQGIIDKIQsgYLTDLGVSAVWISPPfeNITAVDSDIGTsyhgywarDFTDPNEFFGDMETFKQLVDVAHQNGIKVVI 167
Cdd:cd11345  31 GGLKGVEGKLD--YLSQLKVKGLVLGPI--HVVQADQPGEL--------NLTEIDPDLGTLEDFTSLLTAAHKKGISVVL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 168 DFVPNhtspstsdgeledgalydngsyvaaYNDDPKSYFHHNggtdyssyedqiyrnlynladfdhheAYIDQYLKDAIK 247
Cdd:cd11345  99 DLTPN-------------------------YRGESSWAFSDA--------------------------ENVAEKVKEALE 127

                       170       180
                ....*....|....*....|....*...
gi 62816022 248 QWLDAGIDGIRV----DAVAHMPPKWQK 271
Cdd:cd11345 128 FWLNQGVDGIQVsdleNVASSASSEWSN 155
PRK12568 PRK12568
glycogen branching enzyme; Provisional
 89-265 3.13e-06

glycogen branching enzyme; Provisional


Pssm-ID: 139075 [Multi-domain]  Cd Length: 730  Bit Score: 50.72  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   89 DWQGIIDKIQSgYLTDLGVSAVWISPPFENitavdsDIGTSYhGYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVID 168
Cdd:PRK12568 267 DWPTLAEQLIP-YVQQLGFTHIELLPITEH------PFGGSW-GYQPLGLYAPTARHGSPDGFAQFVDACHRAGIGVILD 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  169 FVPNHTsPSTSDG--ELEDGALYDNGsyvaayndDPKSYFHHNggtdyssyedqiyrnlYNLADFDHHEAYIDQYLKDAI 246
Cdd:PRK12568 339 WVSAHF-PDDAHGlaQFDGAALYEHA--------DPREGMHRD----------------WNTLIYNYGRPEVTAYLLGSA 393

                        170       180
                 ....*....|....*....|
gi 62816022  247 KQWLDA-GIDGIRVDAVAHM 265
Cdd:PRK12568 394 LEWIEHyHLDGLRVDAVASM 413
AmyAc_bac_euk_BE cd11321
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching ...
 132-265 4.98e-06

Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic 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: 200460 [Multi-domain]  Cd Length: 406  Bit Score: 49.54  E-value: 4.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 132 GYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTSDGEledgALYDNGSYvaaynddpkSYFHHNGG 211
Cdd:cd11321  71 GYQVTNFFAASSRFGTPEDLKYLIDTAHGMGIAVLLDVVHSHASKNVLDGL----NMFDGTDG---------CYFHEGER 137

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62816022 212 TDYSSYEDQIYrnlynlaDFDHHEayIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:cd11321 138 GNHPLWDSRLF-------NYGKWE--VLRFLLSNLRWWLEEyRFDGFRFDGVTSM 183
TIG pfam01833
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ...
 534-600 1.34e-05

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: 460355 [Multi-domain]  Cd Length: 84  Bit Score: 43.97  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62816022   534 VGPTMGQP--GHTVVLSGDGFG--STEGSVEFGTTSASITSWSNTEIEATVPAVSGGYYDVTVTDANGAQS 600
Cdd:pfam01833   6 ISPSSGPAsgGTTITITGSNFGtdSSDLKVTIGGTPCTVISVSSTTIVCTTPPGTSGLVNVSVTVGGGGIS 76
AmyAc_AGS cd11323
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ...
 53-169 1.36e-05

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 [Multi-domain]  Cd Length: 569  Bit Score: 48.44  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  53 IYQLISDRFRDGNP-NNNPTGELASDDCSNLRKYCGGDWQGIIDKIQsgYLTDLGVSAVWIS-PPFENITavdsdigTSY 130
Cdd:cd11323  58 FYTIFLDRFVNGDPtNDDANGTVFEQDIYETQLRHGGDIVGLVDSLD--YLQGMGIKGIYIAgTPFINMP-------WGA 128

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 62816022 131 HGYWARDFT--DPNefFGDMETFKQLVDVAHQNGIKVVIDF 169
Cdd:cd11323 129 DGYSPLDFTllDHH--FGTIADWRAAIDEIHRRGMYVVLDN 167
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
101-188 1.67e-05

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 48.56  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   101 YLTDLGVSAVWISP-----PfenitavdsdigTSYHGYwarDFTDPNEF---FGDMETFKQLVDVAHQNGIKVVIDFVPN 172
Cdd:PRK14507  766 YLAALGISHVYASPilkarP------------GSTHGY---DIVDHSQInpeIGGEEGFERFCAALKAHGLGQLLDIVPN 830

                          90       100
                  ....*....|....*....|.
gi 62816022   173 HTSPSTSDGE-----LEDGAL 188
Cdd:PRK14507  831 HMGVGGADNPwwldvLENGPA 851
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 529-604 1.96e-05

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 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 529 PALGHVGPTMG--QPGHTVVLSGDGFGSTEGS-VEFGT-TSASITSWSNTEIEATVPAVSG---GYYDVTVTDANGA--- 598
Cdd:cd00102   1 PVITSISPSSGpvSGGTEVTITGSNFGSGSNLrVTFGGgVPCSVLSVSSTAIVCTTPPYANpgpGPVEVTVDRGNGGits 80


                ....*.
gi 62816022 599 QSDPFS 604
Cdd:cd00102  81 SPLTFT 86
AmyAc_Glg_debranch cd11326
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ...
 101-217 2.55e-05

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 [Multi-domain]  Cd Length: 433  Bit Score: 47.08  E-value: 2.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 101 YLTDLGVSAVWISPPFE-NITAVDSDIG-TSYHGYWARDFTDPN-------EFFGDMETFKQLVDVAHQNGIKVVIDFVP 171
Cdd:cd11326  52 YLKELGVTAVELLPVHAfDDEEHLVERGlTNYWGYNTLNFFAPDpryasddAPGGPVDEFKAMVKALHKAGIEVILDVVY 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 62816022 172 NHTspstsdGEL-EDGALY-----DNGSYvaaynddpksYFHHNGGTDYSSY 217
Cdd:cd11326 132 NHT------AEGgELGPTLsfrglDNASY----------YRLDPDGPYYLNY 167
pulA_typeI TIGR02104
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ...
 101-174 5.33e-05

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 [Multi-domain]  Cd Length: 605  Bit Score: 46.54  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   101 YLTDLGVSAVWISPPFENITAVDSDIGTSYH-GYWARDF--------TDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVP 171
Cdd:TIGR02104 172 YLKELGVTHVQLLPVFDFAGVDEEDPNNAYNwGYDPLNYnvpegsysTNPYDPATRIRELKQMIQALHENGIRVIMDVVY 251


                  ...
gi 62816022   172 NHT 174
Cdd:TIGR02104 252 NHT 254
PLN02950 PLN02950
4-alpha-glucanotransferase
 607-710 5.97e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 46.64  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  607 EVLSGDQISARFVVNDATTDVGENVYVVGNVHELGDWDTDRavGPFFNQVVHeyPNWYYDVNLPAGT-DIEFKFVKIASD 685
Cdd:PLN02950 146 KPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDD--GLKLNYTGD--SIWEADCLVPKSDfPIKYKYALQTAE 221

                         90       100
                 ....*....|....*....|....*
gi 62816022  686 GTVTWESGSNRQYTTPTDSTGEYSG 710
Cdd:PLN02950 222 GLVSLELGVNRELSLDSSSGKPPSY 246
PLN02447 PLN02447
1,4-alpha-glucan-branching enzyme
 132-265 2.45e-04

1,4-alpha-glucan-branching enzyme


Pssm-ID: 215246 [Multi-domain]  Cd Length: 758  Bit Score: 44.28  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  132 GYWARDFTDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTSDGeledgalydngsyVAAYNDDPKSYFHhnGG 211
Cdd:PLN02447 283 GYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASKNTLDG-------------LNGFDGTDGSYFH--SG 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62816022  212 tdyssyeDQIYRNLYNLADFDHHEAYIDQYLKDAIKQWLDA-GIDGIRVDAVAHM 265
Cdd:PLN02447 348 -------PRGYHWLWDSRLFNYGNWEVLRFLLSNLRWWLEEyKFDGFRFDGVTSM 395
AmyAc_Pullulanase_LD-like cd11341
Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin ...
 139-174 2.52e-04

Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins; Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of 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: 200480 [Multi-domain]  Cd Length: 406  Bit Score: 44.04  E-value: 2.52e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 62816022 139 TDPNEFFGDMETFKQLVDVAHQNGIKVVIDFVPNHT 174
Cdd:cd11341  97 TDPYDPYARIKEFKEMVQALHKNGIRVIMDVVYNHT 132
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 628-692 3.79e-04

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 40.77  E-value: 3.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62816022 628 GENVYVVGNVHELGDWDTDRAVgpFFNQVVHEYPNWYYDVNLPAGTDIEFKF---VKIASDGTV-----TWES 692
Cdd:cd05814  15 GEVVAVVGSLPVLGNWQPEKAV--PLEKEDDDCNLWKASIELPRGVDFQYRYfvaVVLNDSGPCqvivrKWET 85
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 617-691 5.14e-04

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. 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: 99881  Cd Length: 112  Bit Score: 40.19  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 617 RFVVNDATTDVGENVYVVGNVHELGDWDTDRAV--GPFFNQVVHEYPN-WYYDVNL--PAGTD-IEFKFVKiASDGTVTW 690
Cdd:cd05806   4 RFGVVLTFADRDTELLVLGSRPELGSWDPQRAVpmRPARKALSPQEPSlWLGEVELsePGSEDtFWYKFLK-REAGALIW 82


                .
gi 62816022 691 E 691
Cdd:cd05806  83 E 83
AmyAc_plant_IsoA cd11346
Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching ...
 71-256 6.48e-04

Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like 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: 200484 [Multi-domain]  Cd Length: 347  Bit Score: 42.46  E-value: 6.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  71 TGELASDDCSNLRkycgGDWQGIIDKIqsGYLTDLGVSAVWISPpfenITAVDSDIGTsyhGYWARDFTDPNEFF----- 145
Cdd:cd11346  16 TSHRSAQLPPQHA----GTFLGVLEKV--DHLKSLGVNTVLLQP----IFAFARVKGP---YYPPSFFSAPDPYGagdss 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 146 -GDMETFKQLVDVAHQNGIKVVIDFVPNHTSPSTSDG-ELEDGALYDNGSYvaaYNDDpKSYFHHNGGTDYSSYedqiyr 223
Cdd:cd11346  83 lSASAELRAMVKGLHSNGIEVLLEVVLTHTAEGTDESpESESLRGIDAASY---YILG-KSGVLENSGVPGAAV------ 152

                       170       180       190
                ....*....|....*....|....*....|....
gi 62816022 224 nlynladFDHHEAYIDQYLKDAIKQW-LDAGIDG 256
Cdd:cd11346 153 -------LNCNHPVTQSLILDSLRHWaTEFGVDG 179
PLN00196 PLN00196
alpha-amylase; Provisional
 84-484 1.47e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 41.83  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022   84 KYCGGDWQGIIDKIQSgyLTDLGVSAVWISPPFENItavdsdigtSYHGYWARDFTDPN-EFFGDMETFKQLVDVAHQNG 162
Cdd:PLN00196  37 KQNGGWYNFLMGKVDD--IAAAGITHVWLPPPSHSV---------SEQGYMPGRLYDLDaSKYGNEAQLKSLIEAFHGKG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  163 IKVVIDFVPNHTSPSTSDGEledgalydnGSYVAAYNDDPKSYFH---HNGGTDYSSYEDQIyRNLYNLADF------DH 233
Cdd:PLN00196 106 VQVIADIVINHRTAEHKDGR---------GIYCLFEGGTPDSRLDwgpHMICRDDTQYSDGT-GNLDTGADFaaapdiDH 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  234 HEAYIDQYLKDAIKqWL--DAGIDGIRVDAVAHMPPKWQKTLVDTIydhRPVFTFGE-WFLGADQSNPRYYEFSNDSGMS 310
Cdd:PLN00196 176 LNKRVQRELIGWLL-WLksDIGFDAWRLDFAKGYSAEVAKVYIDGT---EPSFAVAEiWTSMAYGGDGKPEYDQNAHRQE 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  311 LLDF--RFGQEIRQVLR-DFTDDWYgfrdMLQETESEHDQVIDQ---------------VPFIDNHD---------MPRF 363
Cdd:PLN00196 252 LVNWvdRVGGAASPATVfDFTTKGI----LNVAVEGELWRLRGAdgkapgvigwwpakaVTFVDNHDtgstqhmwpFPSD 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022  364 TVADGdtrntdmaLAVLLTSRGTPAVYYgtEQYLTGGNDPDnrkpmpsfdttttaykvIQALTSLRssNRRSPTADTEER 443
Cdd:PLN00196 328 KVMQG--------YAYILTHPGNPCIFY--DHFFDWGLKEE-----------------IAALVSIR--NRNGITPTSELR 378

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 62816022  444 WINSDVFVYEREFGDNVVLVAINRsldwYDVSGLqtsLPEG 484
Cdd:PLN00196 379 IMEADADLYLAEIDGKVIVKIGSR----YDVSHL---IPEG 412
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 614-700 1.73e-03

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99887  Cd Length: 95  Bit Score: 38.25  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62816022 614 ISARFVVNDATTDVGENVYVVGNVHELGDWDTdravgpFFNQVVHEYPNWYYDVNLPAGTDIEFKFVKIASDGTVTWESG 693
Cdd:cd05813   1 VNVTFRVHYITHSDAQLVAVTGDHEELGSWHS------YIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQVTRWEEC 74


                ....*..
gi 62816022 694 SNRQYTT 700
Cdd:cd05813  75 SNRLLET 81
Malt_amylase_C pfam16657
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ...
 446-478 3.57e-03

Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism.


Pssm-ID: 435493 [Multi-domain]  Cd Length: 75  Bit Score: 36.76  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 62816022   446 NSDVFVYEREFGDNVVLVAINRS-----LDWYDVSGLQ 478
Cdd:pfam16657  10 NRKVLAYLREYEDETILVVANRSaqpveLDLSAFEGRV 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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