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Conserved domains on  [gi|618884923|gb|AHX97726|]
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alpha-amylase precursor [Lactiplantibacillus plantarum]

Protein Classification

AmyAc_bac1_AmyA and CBM26 domain-containing protein( domain architecture ID 10877614)

protein containing domains AmyAc_bac1_AmyA, Aamy_C, and CBM26

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 56-402 6.73e-157

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: 464.06  E-value: 6.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  56 DGVILHAWCWSFNTIKNNLKQIHDAGYTAVQTSPVNEVKVGNSASkslNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAA 135
Cdd:cd11315    1 DGVILHAFDWSFNTIKENLPEIAAAGYTAIQTSPPQKSKEGGNEG---GNWWYRYQPTDYRIGNNQLGTEDDFKALCAAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 136 KEYNIRIIVDATLNDTTSDYSAISDEIKSI-------SNWTHGNTQISNWSDREDVTQNSLLGLYDWNTQNSQVQTYLKN 208
Cdd:cd11315   78 HKYGIKIIVDVVFNHMANEGSAIEDLWYPSadielfsPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 209 YLERLISDGASGFRYDAAKHIELPSqyDGSYGSNFWPNITDN---GSEFQYGEVLQDSISKESDYANYMS---VTASNYG 282
Cdd:cd11315  158 YLKALVALGVDGFRFDAAKHIELPD--EPSKASDFWTNILNNldkDGLFIYGEVLQDGGSRDSDYASYLSlggVTASAYG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 283 NTIRNALKNRDFTASTL--QNFNISVPASKLVTWVESHDNYANDDQVSTWMNSSDIKLGWAVVASRSGSVPLFFDRPVDG 360
Cdd:cd11315  236 FPLRGALKNAFLFGGSLdpASYGQALPSDRAVTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGTPLFFSRPNGS 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 618884923 361 GNGTRFpgsseIGDAGSSLYYDKAVVAVNKFHNAMAGQSEYI 402
Cdd:cd11315  316 GGTNPQ-----IGDRGDDAWKSPDVVAVNKFHNAMHGQPEYL 352
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 491-561 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


:

Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  491 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 561
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 597-667 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


:

Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  597 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 667
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 704-774 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


:

Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  704 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 774
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 810-880 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


:

Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  810 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 880
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
Aamy_C smart00632
Aamy_C domain;
402-475 8.56e-11

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 58.79  E-value: 8.56e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 618884923   402 ISNPNGNTKIFENERGSKGVVFANASDGSYSLSVKTSLADGTYENKAG----SDEFTVK-NGYLTGTIQGREVVVLYGD 475
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISglctGKSVTVGsNGIATFTLPAGGAVAIHVD 79
 
Name Accession Description Interval E-value
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 56-402 6.73e-157

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: 464.06  E-value: 6.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  56 DGVILHAWCWSFNTIKNNLKQIHDAGYTAVQTSPVNEVKVGNSASkslNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAA 135
Cdd:cd11315    1 DGVILHAFDWSFNTIKENLPEIAAAGYTAIQTSPPQKSKEGGNEG---GNWWYRYQPTDYRIGNNQLGTEDDFKALCAAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 136 KEYNIRIIVDATLNDTTSDYSAISDEIKSI-------SNWTHGNTQISNWSDREDVTQNSLLGLYDWNTQNSQVQTYLKN 208
Cdd:cd11315   78 HKYGIKIIVDVVFNHMANEGSAIEDLWYPSadielfsPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 209 YLERLISDGASGFRYDAAKHIELPSqyDGSYGSNFWPNITDN---GSEFQYGEVLQDSISKESDYANYMS---VTASNYG 282
Cdd:cd11315  158 YLKALVALGVDGFRFDAAKHIELPD--EPSKASDFWTNILNNldkDGLFIYGEVLQDGGSRDSDYASYLSlggVTASAYG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 283 NTIRNALKNRDFTASTL--QNFNISVPASKLVTWVESHDNYANDDQVSTWMNSSDIKLGWAVVASRSGSVPLFFDRPVDG 360
Cdd:cd11315  236 FPLRGALKNAFLFGGSLdpASYGQALPSDRAVTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGTPLFFSRPNGS 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 618884923 361 GNGTRFpgsseIGDAGSSLYYDKAVVAVNKFHNAMAGQSEYI 402
Cdd:cd11315  316 GGTNPQ-----IGDRGDDAWKSPDVVAVNKFHNAMHGQPEYL 352
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 491-561 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  491 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 561
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 597-667 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  597 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 667
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 704-774 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  704 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 774
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 810-880 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  810 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 880
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 70-332 5.88e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 68.15  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923   70 IKNNLKQIHDAGYTAVQTSPVNEvkvgnsaSKSLNNWYWlyqptkysIGNYY-----LGTEAEFKSMCAAAKEYNIRIIV 144
Cdd:pfam00128   6 IIEKLDYLKELGVTAIWLSPIFD-------SPQADHGYD--------IADYYkidphYGTMEDFKELISKAHERGIKVIL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  145 DATLNDTTSDYSAISDEIKSISN-------WTHGNTQI-----------SNWSDREdVTQNSLL-----GLYDWNTQNSQ 201
Cdd:pfam00128  71 DLVVNHTSDEHAWFQESRSSKDNpyrdyyfWRPGGGPIppnnwrsyfggSAWTYDE-KGQEYYLhlfvaGQPDLNWENPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  202 VQTYLKNYLERLISDGASGFRYDAAKHIELPSQYDGSYGSNFWPNIT---DNGSEFQYGEVLQDSISKESDYANYMSVTA 278
Cdd:pfam00128 150 VRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGPFWHEFTqamNETVFGYKDVMTVGEVFHGDGEWARVYTTE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 618884923  279 SNYGNTIRNALKNRDFTASTLQNFNI-SVPASKLVTWVesHDNYANDDQVSTWMN 332
Cdd:pfam00128 230 ARMELEMGFNFPHNDVALKPFIKWDLaPISARKLKEMI--TDWLDALPDTNGWNF 282
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
114-230 1.94e-11

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 67.20  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 114 KYSIGNYY-----LGTEAEFKSMCAAAKEYNIRIIVDATLNDT--------------TSDYSA---ISDEIKSI--SNWt 169
Cdd:COG0366   62 GYDISDYRdvdprFGTLADFDELVAEAHARGIKVILDLVLNHTsdehpwfqearagpDSPYRDwyvWRDGKPDLppNNW- 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 618884923 170 HGNTQISNWSdREDVTQNSLLGLY-----DWNTQNSQVQTYLKNYLERLISDGASGFRYDAAKHIE 230
Cdd:COG0366  141 FSIFGGSAWT-WDPEDGQYYLHLFfssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLD 205
Aamy smart00642
Alpha-amylase domain;
67-154 2.27e-11

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 63.12  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923    67 FNTIKNNLKQIHDAGYTAVQTSPVNEvkvgnsaSKSLNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAAKEYNIRIIVDA 146
Cdd:smart00642  18 LQGIIEKLDYLKDLGVTAIWLSPIFE-------SPQGYPSYHGYDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDV 90


                   ....*...
gi 618884923   147 TLNDTTSD 154
Cdd:smart00642  91 VINHTSDG 98
Aamy_C smart00632
Aamy_C domain;
402-475 8.56e-11

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 58.79  E-value: 8.56e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 618884923   402 ISNPNGNTKIFENERGSKGVVFANASDGSYSLSVKTSLADGTYENKAG----SDEFTVK-NGYLTGTIQGREVVVLYGD 475
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISglctGKSVTVGsNGIATFTLPAGGAVAIHVD 79
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
79-237 2.08e-03

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


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 42.18  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923   79 DAGYTAVQTSPVNE-VKVGNSASKSLNNwYWLYQPTKYSIGNYYLGTEA--EFKSMCAAAKEYNIRIIVDATLNDT-TSD 154
Cdd:PRK14510  198 KLGVSIVELNPIFAsVDEHHLPQLGLSN-YWGYNTVAFLAPDPRLAPGGeeEFAQAIKEAQSAGIAVILDVVFNHTgESN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  155 YSAISDEIKSISN---WTHG---NTQISNW---SDREDVTQNSLLGLydwntqnsqVQTYLKNYLERlisdGASGFRYDA 225
Cdd:PRK14510  277 HYGPTLSAYGSDNspyYRLEpgnPKEYENWwgcGNLPNLERPFILRL---------PMDVLRSWAKR----GVDGFRLDL 343

                         170
                  ....*....|..
gi 618884923  226 AkhIELPSQYDG 237
Cdd:PRK14510  344 A--DELAREPDG 353
 
Name Accession Description Interval E-value
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 56-402 6.73e-157

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: 464.06  E-value: 6.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  56 DGVILHAWCWSFNTIKNNLKQIHDAGYTAVQTSPVNEVKVGNSASkslNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAA 135
Cdd:cd11315    1 DGVILHAFDWSFNTIKENLPEIAAAGYTAIQTSPPQKSKEGGNEG---GNWWYRYQPTDYRIGNNQLGTEDDFKALCAAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 136 KEYNIRIIVDATLNDTTSDYSAISDEIKSI-------SNWTHGNTQISNWSDREDVTQNSLLGLYDWNTQNSQVQTYLKN 208
Cdd:cd11315   78 HKYGIKIIVDVVFNHMANEGSAIEDLWYPSadielfsPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQQQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 209 YLERLISDGASGFRYDAAKHIELPSqyDGSYGSNFWPNITDN---GSEFQYGEVLQDSISKESDYANYMS---VTASNYG 282
Cdd:cd11315  158 YLKALVALGVDGFRFDAAKHIELPD--EPSKASDFWTNILNNldkDGLFIYGEVLQDGGSRDSDYASYLSlggVTASAYG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 283 NTIRNALKNRDFTASTL--QNFNISVPASKLVTWVESHDNYANDDQVSTWMNSSDIKLGWAVVASRSGSVPLFFDRPVDG 360
Cdd:cd11315  236 FPLRGALKNAFLFGGSLdpASYGQALPSDRAVTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGTPLFFSRPNGS 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 618884923 361 GNGTRFpgsseIGDAGSSLYYDKAVVAVNKFHNAMAGQSEYI 402
Cdd:cd11315  316 GGTNPQ-----IGDRGDDAWKSPDVVAVNKFHNAMHGQPEYL 352
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 57-320 9.30e-35

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: 135.77  E-value: 9.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  57 GVILHAWCWSFNTI----KNNLKqihDAGYTAVQTSPVNEVKVGnsaskSLNNWYWLYQPTKYSIgNYYLGTEAEFKSMC 132
Cdd:cd11317    2 GVIVHLFEWPWNDIakecERFLG---PAGYGGVQVSPPQEHIVG-----PGRPWWERYQPVSYKL-NSRSGTEAEFRDMV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 133 AAAKEYNIRIIVDATLNDTTSDysaisdeiksisnwthgntqisnwsdREDVTQNSLLGLYDWNTQNSQVQTYLKNYLER 212
Cdd:cd11317   73 NRCNAAGVRVYVDAVINHMAGD--------------------------ANEVRNCELVGLADLNTESDYVRDKIADYLND 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 213 LISDGASGFRYDAAKHIelpsqydgsygsnfWPN--------------ITDNGSEFQYGEVL---QDSISKeSDYANYMS 275
Cdd:cd11317  127 LISLGVAGFRIDAAKHM--------------WPEdlaailarlkdlngGPLGSRPYIYQEVIdggGEAIQP-SEYTGNGD 191

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 618884923 276 VTASNYGNTIRNALKNRDfTASTLQNFNIS---VPASKLVTWVESHDN 320
Cdd:cd11317  192 VTEFRYARGLSNAFRGKI-KLLLLKNFGEGwglLPSERAVVFVDNHDN 238
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 70-326 2.74e-22

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: 100.05  E-value: 2.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  70 IKNNLKQIHDAGYTAVQTSPVNEvKVGNSASKSLNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAAKEYNIRIIVDATLN 149
Cdd:cd11320   49 IIDKLPYLKDLGVTAIWISPPVE-NINSPIEGGGNTGYHGYWARDFKRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 150 DTTSD----YSAISDEIKSI-------SNWTHGNTQISNWSDREDVTQNSLLGLYDWNTQNSQVQTYLKNYLERLISDGA 218
Cdd:cd11320  128 HSSPAdyaeDGALYDNGTLVgdypnddNGWFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGI 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 219 SGFRYDAAKHIELPSQydgsygSNFWPNITDNGSEFQYGEVLQDSIS-KESDYANYMSVTASN-----YGNTIRNALKNR 292
Cdd:cd11320  208 DGIRVDAVKHMPPGWQ------KSFADAIYSKKPVFTFGEWFLGSPDpGYEDYVKFANNSGMSlldfpLNQAIRDVFAGF 281

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 618884923 293 DFTASTL-----QNFNISVPASKLVTWVESHD-----NYANDDQ 326
Cdd:cd11320  282 TATMYDLdamlqQTSSDYNYENDLVTFIDNHDmprflTLNNNDK 325
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 42-320 3.03e-19

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: 90.70  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  42 STDDSSNDTADSVSDGVilhaWC-WSFNTIKNNLKQIHDAGYTAVQTSPVNEVKVGNSASKSLNNWYWlyqPTKYSIGNY 120
Cdd:cd11319   20 ARTDGSSTAPCDTADRT----YCgGTWKGIINKLDYIQGMGFDAIWISPIVKNIEGNTAYGEAYHGYW---AQDLYSLNP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 121 YLGTEAEFKSMCAAAKEYNIRIIVDATLNDTTSDYSAISDEIKSISNWT-----HGNTQISNWSDREDVTQ----NSLLG 191
Cdd:cd11319   93 HFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDYSSFVPFNdssyyHPYCWITDYNNQTSVEDcwlgDDVVA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 192 LYDWNTQNSQVQTYLKNYLERLISD-GASGFRYDAAKHIElpsqydgsygSNFWPNITDNGSEFQYGEVLQDSISKESDY 270
Cdd:cd11319  173 LPDLNTENPFVVSTLNDWIKNLVSNySIDGLRIDTAKHVR----------KDFWPGFVEAAGVFAIGEVFDGDPNYVCPY 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 618884923 271 ANYM-SVTasNYG--NTIRNALKNRDFTASTLQNFNISVPASK-----LVTWVESHDN 320
Cdd:cd11319  243 QNYLdGVL--NYPlyYPLVDAFQSTKGSMSALVDTINSVQSSCkdptlLGTFLENHDN 298
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 52-354 1.80e-16

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


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 80.30  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  52 DSVSDGVILHAWCW-SFNTIKNNLKQIHDAGYTAVQTSPVNEvkvgnsaSKSLNNWYWLYQPTKYSIGNYYLGTEAEFKS 130
Cdd:cd00551    8 DRFTDGDSSGGDGGgDLKGIIDKLDYLKDLGVTAIWLTPIFE-------SPEYDGYDKDDGYLDYYEIDPRLGTEEDFKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 131 MCAAAKEYNIRIIVDATLNdttsdysaisdeiksisnwtHgntqisnwsdredvtqnsllglydwntqnsqvqtylkNYL 210
Cdd:cd00551   81 LVKAAHKRGIKVILDLVFN--------------------H-------------------------------------DIL 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 211 ERLISDGASGFRYDAAKHIELPSQYDgsygsnFWPNITDNGSE-----FQYGEVLQDS---ISKESDYANYMSVTASNYG 282
Cdd:cd00551  104 RFWLDEGVDGFRLDAAKHVPKPEPVE------FLREIRKDAKLakpdtLLLGEAWGGPdelLAKAGFDDGLDSVFDFPLL 177

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 618884923 283 NTIRNALKNRDFTASTLQNFNISVPASKLVTW-VESHDNYANDDQVSTWMNSSD---IKLGWAVVASRSGsVPLFF 354
Cdd:cd00551  178 EALRDALKGGEGALAILAALLLLNPEGALLVNfLGNHDTFRLADLVSYKIVELRkarLKLALALLLTLPG-TPMIY 252
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 491-561 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  491 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 561
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 597-667 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  597 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 667
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 704-774 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  704 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 774
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
CBM26 pfam16738
Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.
 810-880 5.05e-12

Starch-binding module 26; CBM26 is a carbohydrate-binding module that binds starch.


Pssm-ID: 407007  Cd Length: 68  Bit Score: 61.91  E-value: 5.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 618884923  810 VYFEKPSSWGsTVYAYVYNKNTNKAITSAWPGKEMTALGNDEYKLDLDTDEDDSdlaVIFTDG-TNQTPAAN 880
Cdd:pfam16738   1 VYFKNPSGWG-TPYIYYWDDSPGSSVGLAWPGVAMTDEGNGWYSYTLPGATSAK---VIFNNGgGNQTPDLN 68
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 70-332 5.88e-12

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


Pssm-ID: 395077 [Multi-domain]  Cd Length: 334  Bit Score: 68.15  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923   70 IKNNLKQIHDAGYTAVQTSPVNEvkvgnsaSKSLNNWYWlyqptkysIGNYY-----LGTEAEFKSMCAAAKEYNIRIIV 144
Cdd:pfam00128   6 IIEKLDYLKELGVTAIWLSPIFD-------SPQADHGYD--------IADYYkidphYGTMEDFKELISKAHERGIKVIL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  145 DATLNDTTSDYSAISDEIKSISN-------WTHGNTQI-----------SNWSDREdVTQNSLL-----GLYDWNTQNSQ 201
Cdd:pfam00128  71 DLVVNHTSDEHAWFQESRSSKDNpyrdyyfWRPGGGPIppnnwrsyfggSAWTYDE-KGQEYYLhlfvaGQPDLNWENPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  202 VQTYLKNYLERLISDGASGFRYDAAKHIELPSQYDGSYGSNFWPNIT---DNGSEFQYGEVLQDSISKESDYANYMSVTA 278
Cdd:pfam00128 150 VRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGPFWHEFTqamNETVFGYKDVMTVGEVFHGDGEWARVYTTE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 618884923  279 SNYGNTIRNALKNRDFTASTLQNFNI-SVPASKLVTWVesHDNYANDDQVSTWMN 332
Cdd:pfam00128 230 ARMELEMGFNFPHNDVALKPFIKWDLaPISARKLKEMI--TDWLDALPDTNGWNF 282
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
114-230 1.94e-11

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 67.20  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 114 KYSIGNYY-----LGTEAEFKSMCAAAKEYNIRIIVDATLNDT--------------TSDYSA---ISDEIKSI--SNWt 169
Cdd:COG0366   62 GYDISDYRdvdprFGTLADFDELVAEAHARGIKVILDLVLNHTsdehpwfqearagpDSPYRDwyvWRDGKPDLppNNW- 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 618884923 170 HGNTQISNWSdREDVTQNSLLGLY-----DWNTQNSQVQTYLKNYLERLISDGASGFRYDAAKHIE 230
Cdd:COG0366  141 FSIFGGSAWT-WDPEDGQYYLHLFfssqpDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLD 205
Aamy smart00642
Alpha-amylase domain;
67-154 2.27e-11

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 63.12  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923    67 FNTIKNNLKQIHDAGYTAVQTSPVNEvkvgnsaSKSLNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAAKEYNIRIIVDA 146
Cdd:smart00642  18 LQGIIEKLDYLKDLGVTAIWLSPIFE-------SPQGYPSYHGYDISDYKQIDPRFGTMEDFKELVDAAHARGIKVILDV 90


                   ....*...
gi 618884923   147 TLNDTTSD 154
Cdd:smart00642  91 VINHTSDG 98
Aamy_C smart00632
Aamy_C domain;
402-475 8.56e-11

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 58.79  E-value: 8.56e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 618884923   402 ISNPNGNTKIFENERGSKGVVFANASDGSYSLSVKTSLADGTYENKAG----SDEFTVK-NGYLTGTIQGREVVVLYGD 475
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVISglctGKSVTVGsNGIATFTLPAGGAVAIHVD 79
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 51-301 4.76e-10

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: 62.60  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  51 ADSVSDGVilhawcWSFNTIKNNLKQIHDAGYTAVQTSPVNEvkvgnSASkslnnwywlYQptKYSIGNYY-----LGTE 125
Cdd:cd11316   12 YDSDGDGI------GDLNGLTEKLDYLNDLGVNGIWLMPIFP-----SPS---------YH--GYDVTDYYaiepdYGTM 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 126 AEFKSMCAAAKEYNIRIIVDATLNDTTSDY----SAISDEIKSISNW--THGNTQISNWSDREDVTQNSLLGLY------ 193
Cdd:cd11316   70 EDFERLIAEAHKRGIKVIIDLVINHTSSEHpwfqEAASSPDSPYRDYyiWADDDPGGWSSWGGNVWHKAGDGGYyygafw 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 194 ----DWNTQNSQVQTYLKNYLERLISDGASGFRYDAAKHI--ELPSQYDGSYGSNFWPNITD-----NGSEFQYGEVLQD 262
Cdd:cd11316  150 sgmpDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIyeNGEGQADQEENIEFWKEFRDyvksvKPDAYLVGEVWDD 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 618884923 263 SiskeSDYANYM-----SVTASNYGNTIRNALKNRDFTASTLQN 301
Cdd:cd11316  230 P----STIAPYYasgldSAFNFDLAEAIIDSVKNGGSGAGLAKA 269
AmyAc_CMD cd11338
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ...
 114-226 2.04e-08

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: 57.49  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 114 KYSIGNYY-----LGTEAEFKSMCAAAKEYNIRIIVDATLNDTTSDYSAISDEIKsisNWTHGNTQISNWSDREDVTQNS 188
Cdd:cd11338   86 KYDTADYFkidphLGTEEDFKELVEEAHKRGIRVILDGVFNHTGDDSPYFQDVLK---YGESSAYQDWFSIYYFWPYFTD 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 618884923 189 LLGLYD----------WNTQNSQVQTYLKNYLERLISDG-ASGFRYDAA 226
Cdd:cd11338  163 EPPNYEswwgvpslpkLNTENPEVREYLDSVARYWLKEGdIDGWRLDVA 211
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 70-319 1.70e-06

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: 51.10  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  70 IKNNLKQIHDAGYTAVQTSPVnevkVGNSASKSLNN---WYWLYQPTKYsigNYYLGTEAEFKSMCAAAKEYNIRIIVDA 146
Cdd:cd11339   47 LIDKLDYIKDLGFTAIWITPV----VKNRSVQAGSAgyhGYWGYDFYRI---DPHLGTDADLQDLIDAAHARGIKVILDI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 147 TLNdttsdysaisdeiksisnwtHGNtqisnwsdredvtqnsllglyDWNTQNSQVQTYLKNYLERLISDGASGFRYDAA 226
Cdd:cd11339  120 VVN--------------------HTG---------------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 227 KHIEL-------PSQYDGSYGSNFwpnitdngseFQYGEVLQDSISKESDYANY---MSVTasNYG--NTIRNALkNRDF 294
Cdd:cd11339  159 KHVPRefwqefaPAIRQAAGKPDF----------FMFGEVYDGDPSYIAPYTTTaggDSVL--DFPlyGAIRDAF-AGGG 225

                        250       260
                 ....*....|....*....|....*....
gi 618884923 295 TASTLQNFNIS----VPASKLVTWVESHD 319
Cdd:cd11339  226 SGDLLQDLFLSddlyNDATELVTFLDNHD 254
AmyAc_4 cd11350
Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ...
 66-319 5.69e-06

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: 49.58  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  66 SFNTIKNNLKQIHDAGYTAVQTSPVNEVKvgnsaskslNNWYWLYQPTKYSIGNYYLGTEAEFKSMCAAAKEYNIRIIVD 145
Cdd:cd11350   31 DFKGVIDKLDYLQDLGVNAIELMPVQEFP---------GNDSWGYNPRHYFALDKAYGTPEDLKRLVDECHQRGIAVILD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 146 ATLNDTTSDYSaisdeIKSISNWTHGNTQISNWSDREDVTQNSLLGLYDWNTQNSQVQTYLKNYLERLIS----DGasgF 221
Cdd:cd11350  102 VVYNHAEGQSP-----LARLYWDYWYNPPPADPPWFNVWGPHFYYVGYDFNHESPPTRDFVDDVNRYWLEeyhiDG---F 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 222 RYDAAKHI-------ELPSQYDGSYgSNFWPNITDNGSE-----FQYGEVLQDSiSKESDYANYMSVT--ASNYgNTIRN 287
Cdd:cd11350  174 RFDLTKGFtqkptggGAWGGYDAAR-IDFLKRYADEAKAvdkdfYVIAEHLPDN-PEETELATYGMSLwgNSNY-SFSQA 250

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 618884923 288 ALKNRDFTASTLQ----NFNISVPASKLVTWVESHD 319
Cdd:cd11350  251 AMGYQGGSLLLDYsgdpYQNGGWSPKNAVNYMESHD 286
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 115-319 7.60e-05

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: 45.78  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 115 YSIGNYY-----LGTEAEFKSMCAAAKEYNIRIIVDATLNDTTSDYSAISDEIKS-------ISNWTHGNTQISNWSDRE 182
Cdd:cd11354   61 YDTLDHYridprLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDgpgseedRWHGHAGGGTPAVFEGHE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 183 DvtqnsLLGLydwNTQNSQVQTYLKNYLERLISDGASGFRYDAAkhielpsqYdgSYGSNFWPNITDNGSE-----FQYG 257
Cdd:cd11354  141 D-----LVEL---DHSDPAVVDMVVDVMCHWLDRGIDGWRLDAA--------Y--AVPPEFWARVLPRVRErhpdaWILG 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 258 EVLQdsiskeSDYANYM------SVTASNYGNTIRNALKNRDF--TASTLQNFNISVPASKLVTWVESHD 319
Cdd:cd11354  203 EVIH------GDYAGIVaasgmdSVTQYELWKAIWSSIKDRNFfeLDWALGRHNEFLDSFVPQTFVGNHD 266
AmyAc_arch_bac_AmyA cd11313
Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ...
 66-226 3.20e-04

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: 44.08  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  66 SFNTIKNNLKQIHDAGYTAVQTSPVNEVKVGNsASKSLNNwywlyqPtkYSIGNYY-----LGTEAEFKSMCAAAKEYNI 140
Cdd:cd11313   20 TFKAVTKDLPRLKDLGVDILWLMPIHPIGEKN-RKGSLGS------P--YAVKDYRavnpeYGTLEDFKALVDEAHDRGM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923 141 RIIVDATLNDTTSDySAISDEIKSISNWTHGNTQISNWSDREDVtqnsllglYDWNTQNSQVQTYLKNYLERLISD-GAS 219
Cdd:cd11313   91 KVILDWVANHTAWD-HPLVEEHPEWYLRDSDGNITNKVFDWTDV--------ADLDYSNPELRDYMIDAMKYWVREfDVD 161


                 ....*..
gi 618884923 220 GFRYDAA 226
Cdd:cd11313  162 GFRCDVA 168
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
79-237 2.08e-03

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


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 42.18  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923   79 DAGYTAVQTSPVNE-VKVGNSASKSLNNwYWLYQPTKYSIGNYYLGTEA--EFKSMCAAAKEYNIRIIVDATLNDT-TSD 154
Cdd:PRK14510  198 KLGVSIVELNPIFAsVDEHHLPQLGLSN-YWGYNTVAFLAPDPRLAPGGeeEFAQAIKEAQSAGIAVILDVVFNHTgESN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 618884923  155 YSAISDEIKSISN---WTHG---NTQISNW---SDREDVTQNSLLGLydwntqnsqVQTYLKNYLERlisdGASGFRYDA 225
Cdd:PRK14510  277 HYGPTLSAYGSDNspyYRLEpgnPKEYENWwgcGNLPNLERPFILRL---------PMDVLRSWAKR----GVDGFRLDL 343

                         170
                  ....*....|..
gi 618884923  226 AkhIELPSQYDG 237
Cdd:PRK14510  344 A--DELAREPDG 353
 
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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