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Conserved domains on  [gi|58044330|gb|AAW64454|]
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AMYREL [Drosophila flavohirta]

Protein Classification

alpha-amylase family protein( domain architecture ID 10183021)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 29-398 0e+00

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


:

Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 522.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  29 RNTIVHLFEWKWTDIAEECENFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGDKKEFADMVRRCNDVGI 108
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 109 RIYVDVLLNHMSGDfdgvavgtagtkaepskksfpgvpfsaqdfhpsceiydwndRFQVQQCELVGLKDLDQSSGYVRSK 188
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 189 LIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSLSNLNinhGFPHNARAFIFQEVIDHGHETVSRDEYKDLGAVTEFR 268
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 269 FSEEIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRD---MGAVLNYKTPKQYKMATAFHLAYPYGISRVMS 345
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGhggGGDMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 58044330 346 SFAFDDHDTPPPQDAEERIISPQFNEEGACLNGWICEHRWRQIYAMVGFKNAV 398
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
405-492 9.06e-35

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 125.04  E-value: 9.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330    405 EWWDNGDNQISFCRGNKGFLAVNNNLYDLSQHLNTCLPAGTYCDVISgslinGSCTGKSVTVNDQGYGYIHIGSqdfDGV 484
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 58044330    485 LALHVDAK 492
Cdd:smart00632  74 VAIHVDAK 81
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 29-398 0e+00

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 522.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  29 RNTIVHLFEWKWTDIAEECENFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGDKKEFADMVRRCNDVGI 108
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 109 RIYVDVLLNHMSGDfdgvavgtagtkaepskksfpgvpfsaqdfhpsceiydwndRFQVQQCELVGLKDLDQSSGYVRSK 188
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 189 LIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSLSNLNinhGFPHNARAFIFQEVIDHGHETVSRDEYKDLGAVTEFR 268
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 269 FSEEIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRD---MGAVLNYKTPKQYKMATAFHLAYPYGISRVMS 345
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGhggGGDMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 58044330 346 SFAFDDHDTPPPQDAEERIISPQFNEEGACLNGWICEHRWRQIYAMVGFKNAV 398
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
405-492 9.06e-35

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 125.04  E-value: 9.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330    405 EWWDNGDNQISFCRGNKGFLAVNNNLYDLSQHLNTCLPAGTYCDVISgslinGSCTGKSVTVNDQGYGYIHIGSqdfDGV 484
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 58044330    485 LALHVDAK 492
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
31-122 2.02e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.10  E-value: 2.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330     31 TIVHLFEWK-------WTDIAEECEnFLAPRGFAGVQVSPVNENIIsaGRPWWERYQPISYK-LTTRSGDKKEFADMVRR 102
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 58044330    103 CNDVGIRIYVDVLLNHMSGD 122
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 408-490 5.78e-17

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 75.84  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   408 DNGDNQISFCRGN---KGFLAVNNNLYDLSQHLNTCLP-AGTYCDVISGSLIN--GSCTGKSVTVNDQGYGYIHIGSQDF 481
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 58044330   482 DGVLALHVD 490
Cdd:pfam02806  86 LSALVLKVE 94
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
91-337 4.68e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 76.83  E-value: 4.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  91 GDKKEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTAGTK------AEPSKKSFPGVPFSaqDFHPSCEIYDW 161
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEhpwFQEARAGPDSPYrdwyvwRDGKPDLPPNNWFS--IFGGSAWTWDP 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 162 ND------RFqvqqceLVGLKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMaSEDLkyiyGSLSNLNINHGF-- 233
Cdd:COG0366 154 EDgqyylhLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHL-DKDE----GLPENLPEVHEFlr 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 234 -------PHNARAFIFQEVIDHGHETVSR----DEykdLGAVTEFRFSEEIGNAFRGNNALKW---LQSWGTGWGflPSG 299
Cdd:COG0366 223 elraavdEYYPDFFLVGEAWVDPPEDVARyfggDE---LDMAFNFPLMPALWDALAPEDAAELrdaLAQTPALYP--EGG 297

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 58044330 300 QALTFVDNHDNQRDMGAVLNYKTPKQYKMATAFHLAYP 337
Cdd:COG0366 298 WWANFLRNHDQPRLASRLGGDYDRRRAKLAAALLLTLP 335
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 84-332 1.64e-11

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: 65.46  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330    84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGtKAEPSKKSFPGVPfSAQDFHPSCEI----- 158
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSS-KDNPYRDYYFWRP-GGGPIPPNNWRsyfgg 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   159 YDWNDRFQVQQCEL----VGLKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYgslSNLNINHGFP 234
Cdd:pfam00128 120 SAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFWHEFT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   235 H--NARAFIFQEVI------------------DHGHETVSRDEYKDLGAVTEFRFSEEIGNAfrgnNALKWlQSWGTGW- 293
Cdd:pfam00128 197 QamNETVFGYKDVMtvgevfhgdgewarvyttEARMELEMGFNFPHNDVALKPFIKWDLAPI----SARKL-KEMITDWl 271

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 58044330   294 GFLPSGQ--ALTFVDNHDNQRdmgaVLNY--KTPKQYKMATAF 332
Cdd:pfam00128 272 DALPDTNgwNFTFLGNHDQPR----FLSRfgDDRASAKLLAVF 310
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 88-313 1.48e-06

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 50.66  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   88 TRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSG-------------------------------DFDGVAVGTAGTKAE 136
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadeketfrvvevdpddrtqiisepyeiegwtRFTFPGRGGKYSDFK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  137 PSKKSFPGVPFSAQD-----FHPSCEIYDWNDrfQVQQcELVGL-----KDLDQSSGYVRSKLIEFLDHLIE-LGVAGFR 205
Cdd:PRK09441 155 WHWYHFSGTDYDENPdesgiFKIVGDGKGWDD--QVDD-ENGNFdylmgADIDFRHPEVREELKYWAKWYMEtTGFDGFR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  206 VDAAKHMasedlkyiygslsnlninhgfphnaRAFIFQEVIDHGHETVSRDEYkdlgAVTEF---------RFSEEIG-- 274
Cdd:PRK09441 232 LDAVKHI-------------------------DAWFIKEWIEHVREVAGKDLF----IVGEYwshdvdklqDYLEQVEgk 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 58044330  275 -------------NAFRGNNA--LKWLQSwGTGWGFLPSgQALTFVDNHDNQRD 313
Cdd:PRK09441 283 tdlfdvplhynfhEASKQGRDydMRNIFD-GTLVEADPF-HAVTFVDNHDTQPG 334
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 29-398 0e+00

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 522.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  29 RNTIVHLFEWKWTDIAEECENFLAPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGDKKEFADMVRRCNDVGI 108
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEHIVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 109 RIYVDVLLNHMSGDfdgvavgtagtkaepskksfpgvpfsaqdfhpsceiydwndRFQVQQCELVGLKDLDQSSGYVRSK 188
Cdd:cd11317  81 RVYVDAVINHMAGD-----------------------------------------ANEVRNCELVGLADLNTESDYVRDK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 189 LIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSLSNLNinhGFPHNARAFIFQEVIDHGHETVSRDEYKDLGAVTEFR 268
Cdd:cd11317 120 IADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLN---GGPLGSRPYIYQEVIDGGGEAIQPSEYTGNGDVTEFR 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 269 FSEEIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRD---MGAVLNYKTPKQYKMATAFHLAYPYGISRVMS 345
Cdd:cd11317 197 YARGLSNAFRGKIKLLLLKNFGEGWGLLPSERAVVFVDNHDNQRGhggGGDMLTYKDGRRYKLANAFMLAWPYGTPRVMS 276

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 58044330 346 SFAFDDHDTPPPQDAEERIISPQFNEEGACLNGWICEHRWRQIYAMVGFKNAV 398
Cdd:cd11317 277 SYYFSDSDQGPPSDGSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 31-398 7.61e-53

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: 182.09  E-value: 7.61e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  31 TIVHLFEWKWTDIAEECENfLAPRGFAGVQVSPVNENI--ISAGRPWWERYQPISYKLTTRS-GDKKEFADMVRRCNDVG 107
Cdd:cd11315   3 VILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKegGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 108 IRIYVDVLLNHMSGDFDGVAVgtagtkaePSKKSFPGVPFSAQDFHPSCEIYDWNDRFQVQQCELVGLKDLDQSSGYVRS 187
Cdd:cd11315  82 IKIIVDVVFNHMANEGSAIED--------LWYPSADIELFSPEDFHGNGGISNWNDRWQVTQGRLGGLPDLNTENPAVQQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 188 KLIEFLDHLIELGVAGFRVDAAKHMASEDLKYiYGSLSNLNINHGFPHNARaFIFQEVIDhghETVSRDE----YKDLGA 263
Cdd:cd11315 154 QQKAYLKALVALGVDGFRFDAAKHIELPDEPS-KASDFWTNILNNLDKDGL-FIYGEVLQ---DGGSRDSdyasYLSLGG 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 264 VTEFRFSEEIGNAFRGNNAL---KWLQSWGTGwgfLPSGQALTFVDNHDNQRDMGAVLNYKTPKQYKMATAFHLAYPYGI 340
Cdd:cd11315 229 VTASAYGFPLRGALKNAFLFggsLDPASYGQA---LPSDRAVTWVESHDTYNNDGFESTGLDDEDERLAWAYLAARDGGT 305

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58044330 341 SRVmssfaFDDHDtpppqdaeeriispqfneEGACLNGWICEhRWRQIY------AMVGFKNAV 398
Cdd:cd11315 306 PLF-----FSRPN------------------GSGGTNPQIGD-RGDDAWkspdvvAVNKFHNAM 345
Aamy_C smart00632
Aamy_C domain;
405-492 9.06e-35

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 125.04  E-value: 9.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330    405 EWWDNGDNQISFCRGNKGFLAVNNNLYDLSQHLNTCLPAGTYCDVISgslinGSCTGKSVTVNDQGYGYIHIGSqdfDGV 484
Cdd:smart00632   2 NWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPA---GGA 73


                   ....*...
gi 58044330    485 LALHVDAK 492
Cdd:smart00632  74 VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
31-122 2.02e-26

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 105.10  E-value: 2.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330     31 TIVHLFEWK-------WTDIAEECEnFLAPRGFAGVQVSPVNENIIsaGRPWWERYQPISYK-LTTRSGDKKEFADMVRR 102
Cdd:smart00642   2 IYPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESPQ--GYPSYHGYDISDYKqIDPRFGTMEDFKELVDA 78

                           90       100
                   ....*....|....*....|
gi 58044330    103 CNDVGIRIYVDVLLNHMSGD 122
Cdd:smart00642  79 AHARGIKVILDVVINHTSDG 98
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 55-354 1.72e-21

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: 96.20  E-value: 1.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  55 GFAGVQVSPVNENI-------ISAGrpwWERYQPISYKLTTRS-GDKKEFADMVRRCNDVGIRIYVDVLLNHmSGDFDgv 126
Cdd:cd11320  60 GVTAIWISPPVENInspieggGNTG---YHGYWARDFKRTNEHfGTWEDFDELVDAAHANGIKVIIDFVPNH-SSPAD-- 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 127 avgTAGTKAEPSKKSF-PGVPFSAQD-FHPSCEIYDWNDRFQVQQCELVGLKDLDQSSGYVRSKLIEFLDHLIELGVAGF 204
Cdd:cd11320 134 ---YAEDGALYDNGTLvGDYPNDDNGwFHHNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKDAIKFWLDHGIDGI 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 205 RVDAAKHMASEDLK----YIYGSLSnlninhgfphnarAFIFQEVIDHGHETVSRDEYKDLG----AVTEFRFSEEIGNA 276
Cdd:cd11320 211 RVDAVKHMPPGWQKsfadAIYSKKP-------------VFTFGEWFLGSPDPGYEDYVKFANnsgmSLLDFPLNQAIRDV 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 277 FRGNNALKW-----LQSwgTGWGFLPSGQALTFVDNHDNQRDMGAVLNYKTpkqYKMATAFHLAYP------YGISRVMS 345
Cdd:cd11320 278 FAGFTATMYdldamLQQ--TSSDYNYENDLVTFIDNHDMPRFLTLNNNDKR---LHQALAFLLTSRgipviyYGTEQYLH 352


                ....*....
gi 58044330 346 SFAFDDHDT 354
Cdd:cd11320 353 GGTQVGGDP 361
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 55-332 1.97e-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: 89.93  E-value: 1.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  55 GFAGVQVSPVNENIiSAGRPWWERY-----QPIsYKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMsgdfdgvavG 129
Cdd:cd11319  56 GFDAIWISPIVKNI-EGNTAYGEAYhgywaQDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM---------A 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 130 TAGTKAEPSKKSFpgVPFSAQ-DFHPSCEIYDWNDRFQVQQCEL----VGLKDLDQSSGYVRSKLIEFLDHLI-ELGVAG 203
Cdd:cd11319 125 SAGPGSDVDYSSF--VPFNDSsYYHPYCWITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDG 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 204 FRVDAAKHMASEDLKyiygslsnlninhGFPHNARAFIFQEVIDHGHETVSrdEYKD-LGAVTEF--------RFSEEIG 274
Cdd:cd11319 203 LRIDTAKHVRKDFWP-------------GFVEAAGVFAIGEVFDGDPNYVC--PYQNyLDGVLNYplyyplvdAFQSTKG 267

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 58044330 275 NAFRGNNALKWLQSwgtgwGFLPSGQALTFVDNHDNQRdmgaVLNYKT-PKQYKMATAF 332
Cdd:cd11319 268 SMSALVDTINSVQS-----SCKDPTLLGTFLENHDNPR----FLSYTSdQALAKNALAF 317
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 408-490 5.78e-17

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


Pssm-ID: 426991 [Multi-domain]  Cd Length: 94  Bit Score: 75.84  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   408 DNGDNQISFCRGN---KGFLAVNNNLYDLSQHLNTCLP-AGTYCDVISGSLIN--GSCTGKSVTVNDQGYGYIHIGSQDF 481
Cdd:pfam02806   6 DAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLTLTLPP 85


                  ....*....
gi 58044330   482 DGVLALHVD 490
Cdd:pfam02806  86 LSALVLKVE 94
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 26-337 6.45e-17

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: 80.68  E-value: 6.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  26 WGNRNTIVHLFEWKWTDIAEECEnFLAPRGFAGVQVSPVNENIiSAGRPWWERYQPISYKLTTRSGDKKEFADMVRRCND 105
Cdd:cd00551  10 FTDGDSSGGDGGGDLKGIIDKLD-YLKDLGVTAIWLTPIFESP-EYDGYDKDDGYLDYYEIDPRLGTEEDFKELVKAAHK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 106 VGIRIYVDVLLNHmsgdfdgvavgtagtkaepskksfpgvpfsaqdfhpsceiydwndrfqvqqcelvglkdldqssgyv 185
Cdd:cd00551  88 RGIKVILDLVFNH------------------------------------------------------------------- 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 186 rskliEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSLsnlnINHGFPHNARAFIFQEVIDHGHETVSRDEYKD-LGAV 264
Cdd:cd00551 101 -----DILRFWLDEGVDGFRLDAAKHVPKPEPVEFLREI----RKDAKLAKPDTLLLGEAWGGPDELLAKAGFDDgLDSV 171

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58044330 265 TEFRFSEEIGNAFRGNNaLKWLQSWGTGWGFLPSGQALTFVDNHDNQRDMGAVLNYKTP---KQYKMATAFHLAYP 337
Cdd:cd00551 172 FDFPLLEALRDALKGGE-GALAILAALLLLNPEGALLVNFLGNHDTFRLADLVSYKIVElrkARLKLALALLLTLP 246
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
91-337 4.68e-15

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 76.83  E-value: 4.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  91 GDKKEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTAGTK------AEPSKKSFPGVPFSaqDFHPSCEIYDW 161
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSDEhpwFQEARAGPDSPYrdwyvwRDGKPDLPPNNWFS--IFGGSAWTWDP 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 162 ND------RFqvqqceLVGLKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMaSEDLkyiyGSLSNLNINHGF-- 233
Cdd:COG0366 154 EDgqyylhLF------FSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHL-DKDE----GLPENLPEVHEFlr 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 234 -------PHNARAFIFQEVIDHGHETVSR----DEykdLGAVTEFRFSEEIGNAFRGNNALKW---LQSWGTGWGflPSG 299
Cdd:COG0366 223 elraavdEYYPDFFLVGEAWVDPPEDVARyfggDE---LDMAFNFPLMPALWDALAPEDAAELrdaLAQTPALYP--EGG 297

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 58044330 300 QALTFVDNHDNQRDMGAVLNYKTPKQYKMATAFHLAYP 337
Cdd:COG0366 298 WWANFLRNHDQPRLASRLGGDYDRRRAKLAAALLLTLP 335
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 84-314 1.77e-12

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: 68.43  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSgdfdgvavgtagtkaepskksfpgvpfsaqdfhpsceiydwnd 163
Cdd:cd11339  89 YRIDPHLGTDADLQDLIDAAHARGIKVILDIVVNHTG------------------------------------------- 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 164 rfqvqqcelvglkDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSLSNLNINHGFphnaraFIFQ 243
Cdd:cd11339 126 -------------DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVPREFWQEFAPAIRQAAGKPDF------FMFG 186

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58044330 244 EVIDHGHETVSR-DEYKDLGAVTEFRFSEEIGNAFRGNNALKWLQSW-GTGWGFLPSGQALTFVDNHDNQRDM 314
Cdd:cd11339 187 EVYDGDPSYIAPyTTTAGGDSVLDFPLYGAIRDAFAGGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGRFL 259
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 84-332 1.64e-11

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: 65.46  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330    84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGtKAEPSKKSFPGVPfSAQDFHPSCEI----- 158
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTSDEHAWFQESRSS-KDNPYRDYYFWRP-GGGPIPPNNWRsyfgg 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   159 YDWNDRFQVQQCEL----VGLKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYgslSNLNINHGFP 234
Cdd:pfam00128 120 SAWTYDEKGQEYYLhlfvAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFE---NNGPFWHEFT 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   235 H--NARAFIFQEVI------------------DHGHETVSRDEYKDLGAVTEFRFSEEIGNAfrgnNALKWlQSWGTGW- 293
Cdd:pfam00128 197 QamNETVFGYKDVMtvgevfhgdgewarvyttEARMELEMGFNFPHNDVALKPFIKWDLAPI----SARKL-KEMITDWl 271

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 58044330   294 GFLPSGQ--ALTFVDNHDNQRdmgaVLNY--KTPKQYKMATAF 332
Cdd:pfam00128 272 DALPDTNgwNFTFLGNHDQPR----FLSRfgDDRASAKLLAVF 310
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 84-318 2.59e-08

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: 55.80  E-value: 2.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVAVGTAGTKAEPSKKSFPGVPfsaqDFHPSC-EIYDWn 162
Cdd:cd11354  67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRSHPAVAQALEDGPGSEEDRWHGHAG----GGTPAVfEGHED- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 163 drfqvqqcelvgLKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLKYIYGSlsnlnINHGFPHnarAFIF 242
Cdd:cd11354 142 ------------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDAAYAVPPEFWARVLPR-----VRERHPD---AWIL 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 243 QEVIdHGHE-TVSRDEYKDlgAVTEFRFSEEIGNAFRGNNAlkWLQSWGTGW--GFLPSGQALTFVDNHDNQR------D 313
Cdd:cd11354 202 GEVI-HGDYaGIVAASGMD--SVTQYELWKAIWSSIKDRNF--FELDWALGRhnEFLDSFVPQTFVGNHDVTRiasqvgD 276


                ....*
gi 58044330 314 MGAVL 318
Cdd:cd11354 277 DGAAL 281
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 88-313 1.48e-06

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 50.66  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   88 TRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSG-------------------------------DFDGVAVGTAGTKAE 136
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadeketfrvvevdpddrtqiisepyeiegwtRFTFPGRGGKYSDFK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  137 PSKKSFPGVPFSAQD-----FHPSCEIYDWNDrfQVQQcELVGL-----KDLDQSSGYVRSKLIEFLDHLIE-LGVAGFR 205
Cdd:PRK09441 155 WHWYHFSGTDYDENPdesgiFKIVGDGKGWDD--QVDD-ENGNFdylmgADIDFRHPEVREELKYWAKWYMEtTGFDGFR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  206 VDAAKHMasedlkyiygslsnlninhgfphnaRAFIFQEVIDHGHETVSRDEYkdlgAVTEF---------RFSEEIG-- 274
Cdd:PRK09441 232 LDAVKHI-------------------------DAWFIKEWIEHVREVAGKDLF----IVGEYwshdvdklqDYLEQVEgk 282

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 58044330  275 -------------NAFRGNNA--LKWLQSwGTGWGFLPSgQALTFVDNHDNQRD 313
Cdd:PRK09441 283 tdlfdvplhynfhEASKQGRDydMRNIFD-GTLVEADPF-HAVTFVDNHDTQPG 334
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 84-337 6.49e-06

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


Pssm-ID: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 47.99  E-value: 6.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSGDFDGVavgtagtkaepskkSFPGVPfsaqdfhpsceiydwnd 163
Cdd:cd11314  57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGPDTGE--------------DFGGAP----------------- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 164 rfqvqqcelvglkDLDQSSGYVRSKLIEFLDHLI-ELGVAGFRVDAAKHMASEDLKyIY-----GSLS------NLNINH 231
Cdd:cd11314 106 -------------DLDHTNPEVQNDLKAWLNWLKnDIGFDGWRFDFVKGYAPSYVK-EYneatsPSFSvgeywdGLSYEN 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 232 GFPHnarafiFQEVIDHGHETvsrdeyKDLGAVTEFRFSEEIGNAFrgNNALKWLQSWGTG-----WGFLPSGqALTFVD 306
Cdd:cd11314 172 QDAH------RQRLVDWIDAT------GGGSAAFDFTTKYILQEAV--NNNEYWRLRDGQGkppglIGWWPQK-AVTFVD 236

                       250       260       270
                ....*....|....*....|....*....|..
gi 58044330 307 NHDNQRDMGavlNYKTPKQYKM-ATAFHLAYP 337
Cdd:cd11314 237 NHDTGSTQG---HWPFPTDNVLqGYAYILTHP 265
PLN02784 PLN02784
alpha-amylase
 36-309 1.23e-05

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 48.08  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330   36 FEW------KWTDIAEECENFLAPRGFAGVQVSPVNENIISAGrpwwerYQPIS-YKLTTRSGDKKEFADMVRRCNDVGI 108
Cdd:PLN02784 509 FNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVSPEG------YMPKDlYNLNSRYGTIDELKDLVKSFHEVGI 582

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  109 RIYVDVLLNHMSGDFdgvavgtagtkaepskKSFPGV--PFSAQdfhpsceiYDWNDR--------FQVQQCELVG---- 174
Cdd:PLN02784 583 KVLGDAVLNHRCAHF----------------QNQNGVwnIFGGR--------LNWDDRavvaddphFQGRGNKSSGdnfh 638

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  175 -LKDLDQSSGYVRSKLIEFLDHLI-ELGVAGFRVDAAK---------HM-ASE----------DLKYIYGSLSN------ 226
Cdd:PLN02784 639 aAPNIDHSQDFVRKDLKEWLCWMRkEVGYDGWRLDFVRgfwggyvkdYMeASEpyfavgeywdSLSYTYGEMDYnqdahr 718

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  227 ------LNINHGfphNARAFifqEVIDHG--HETVSRDEYkdlgavteFRFSEEIGNAfrgNNALKWlqsWgtgwgflPS 298
Cdd:PLN02784 719 qrivdwINATNG---TAGAF---DVTTKGilHSALERCEY--------WRLSDQKGKP---PGVVGW---W-------PS 771

                        330
                 ....*....|.
gi 58044330  299 gQALTFVDNHD 309
Cdd:PLN02784 772 -RAVTFIENHD 781
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 185-331 3.87e-05

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: 46.04  E-value: 3.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 185 VRSKLIEFLDHLIELGVAGFRVDAAKHMASEdlkyiYGSLSNLNINHGFPH---------NARAFIFQEVIDHGhETVSR 255
Cdd:cd11316 162 VREEIKKIAKFWLDKGVDGFRLDAAKHIYEN-----GEGQADQEENIEFWKefrdyvksvKPDAYLVGEVWDDP-STIAP 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 256 DEYKDLGAVTEFRFSEEIG----NAFRGNNALKWLQSW-GTGWGFLPSGQALTFVDNHDNQRDMGAVLNykTPKQYKMAT 330
Cdd:cd11316 236 YYASGLDSAFNFDLAEAIIdsvkNGGSGAGLAKALLRVyELYAKYNPDYIDAPFLSNHDQDRVASQLGG--DEAKAKLAA 313


                .
gi 58044330 331 A 331
Cdd:cd11316 314 A 314
AmyAc_TreS cd11334
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ...
 84-212 6.37e-05

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: 45.25  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  84 YKLTTRSGDKKEFADMVRRCNDVGIRIYVDVLLNHMSGD---FDGVAVGTAGT-------KAEPSKKS-----FPGVPFS 148
Cdd:cd11334  65 YGVDPRLGTLGDFVEFLREAHERGIRVIIDLVVNHTSDQhpwFQAARRDPDSPyrdyyvwSDTPPKYKdariiFPDVEKS 144

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58044330 149 AQDFHPSCEIYDWNdRFQVQQcelvglKDLDQSSGYVRSKLIEFLDHLIELGVAGFRVDAAKHM 212
Cdd:cd11334 145 NWTWDEVAGAYYWH-RFYSHQ------PDLNFDNPAVREEILRIMDFWLDLGVDGFRLDAVPYL 201
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 88-313 4.80e-04

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


Pssm-ID: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 42.50  E-value: 4.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330  88 TRSGDKKEFADMVRRCNDVGIRIYVDVLLNH-MSGD----FDGVAVGTAGTKAEPSKK---------SFPG-------VP 146
Cdd:cd11318  73 TKYGTKEELLEAIKALHENGIQVYADAVLNHkAGADetetVKAVEVDPNDRNKEISEPyeieawtkfTFPGrggkysdFK 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 147 FSAQDFHPSceiyDWNDR------FQVQQC-----ELVGLK----------DLDQSSGYVRSKLIE----FLDhliELGV 201
Cdd:cd11318 153 WNWQHFSGV----DYDQKtkkkgiFKINFEgkgwdEDVDDEngnydylmgaDIDYSNPEVREELKRwgkwYIN---TTGL 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58044330 202 AGFRVDAAKHmasedlkyiygslsnlnINHGFphnarafiFQEVIDHGHETVSRD-----EY--KDLGAVTEF------- 267
Cdd:cd11318 226 DGFRLDAVKH-----------------ISASF--------IKDWIDHLRRETGKDlfavgEYwsGDLEALEDYldatdgk 280

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 58044330 268 ----------RFSEeignAFRGNNALKWLQSWGtgwGFLPSG---QALTFVDNHDNQRD 313
Cdd:cd11318 281 mslfdvplhyNFHE----ASKSGGNYDLRKIFD---GTLVQSrpdKAVTFVDNHDTQPG 332
 
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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