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Conserved domains on  [gi|10280622|ref|NP_066188|]
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alpha-amylase 2B precursor [Homo sapiens]

Protein Classification

alpha-amylase family protein( domain architecture ID 10183021)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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


:

Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 578.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 105 GVRIYVDAVINHMSGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317  79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 185 LEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317 111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317 189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10280622 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317 266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.21e-30

Aamy_C domain;


:

Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622    422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 10280622    502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
PLN02447 super family cl33494
1,4-alpha-glucan-branching enzyme
 85-155 4.20e-03

1,4-alpha-glucan-branching enzyme


The actual alignment was detected with superfamily member PLN02447:

Pssm-ID: 215246 [Multi-domain]  Cd Length: 758  Bit Score: 39.66  E-value: 4.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10280622   85 CTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAVS--AGTSSTCGSYFNPGSRDFPAVpysgWD---FNDGK 155
Cdd:PLN02447 293 SSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASKNTLDglNGFDGTDGSYFHSGPRGYHWL----WDsrlFNYGN 364
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 578.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 105 GVRIYVDAVINHMSGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317  79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 185 LEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317 111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317 189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10280622 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317 266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
Aamy_C smart00632
Aamy_C domain;
422-510 2.21e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622    422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 10280622    502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 8.65e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 106.26  E-value: 8.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622     28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 10280622    100 RCNNVGVRIYVDAVINHMSGN 120
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 421-508 9.84e-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: 75.45  E-value: 9.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 10280622   495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 1.71e-14

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: 74.70  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622    82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSgnavsagtssTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTS----------DEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   161 GDIENYNDATQVRDCR----------LVGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   231 NLNSNWFPAGSKPFIYQEVIDLG------GEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEKMSY--LKNWGEG 298
Cdd:pfam00128 191 FWHEFTQAMNETVFGYKDVMTVGevfhgdGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPISArkLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 10280622   299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 1.69e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 69.12  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMS------GNAVSAGTSSTcgsyfnpgsRDFpavpYSGWDFNDGKCKTGSGD 162
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSdehpwfQEARAGPDSPY---------RDW----YVWRDGKPDLPPNNWFS 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 163 IENYNDATQVRDCR-------LVGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKLH 230
Cdd:COG0366 143 IFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLR 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 231 NLNSNWFPAGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSDR 306
Cdd:COG0366 223 ELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEGG 297

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 10280622 307 ALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366 298 WWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
PLN02784 PLN02784
alpha-amylase
 21-332 8.08e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 51.94  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   21 TQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   94 FRNMVTRCNNVGVRIYVDAVINHMSGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNYNDATQV 172
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NFHAAPNI 643

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  173 RDcrlvglldlalEKDYVRSKIAEYMNHLID-IGVAGFRLDASKHMWPGDIKAILDKlhnlNSNWFPAG----SKPFIY- 246
Cdd:PLN02784 644 DH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYMEA----SEPYFAVGeywdSLSYTYg 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  247 ----------QEVIDLggepIKSSdyfgNGRVTEFKYGAK--LGTVIRKWNGEKMSYLKNWGEG-WGFMPSdRALVFVDN 313
Cdd:PLN02784 709 emdynqdahrQRIVDW----INAT----NGTAGAFDVTTKgiLHSALERCEYWRLSDQKGKPPGvVGWWPS-RAVTFIEN 779

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 10280622  314 HD--NQRGHG--------AGGASILT-------FWD 332
Cdd:PLN02784 780 HDtgSTQGHWrfpegkemQGYAYILThpgtpavFYD 815
PLN02447 PLN02447
1,4-alpha-glucan-branching enzyme
 85-155 4.20e-03

1,4-alpha-glucan-branching enzyme


Pssm-ID: 215246 [Multi-domain]  Cd Length: 758  Bit Score: 39.66  E-value: 4.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10280622   85 CTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAVS--AGTSSTCGSYFNPGSRDFPAVpysgWD---FNDGK 155
Cdd:PLN02447 293 SSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASKNTLDglNGFDGTDGSYFHSGPRGYHWL----WDsrlFNYGN 364
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 25-416 0e+00

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


Pssm-ID: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 578.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  25 RTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENvaIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNV 104
Cdd:cd11317   1 RGVIVHLFEWPWNDIAKECERFLGPAGYGGVQVSPPQEH--IVGPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 105 GVRIYVDAVINHMSGnavsagtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienynDATQVRDCRLVGLLDLA 184
Cdd:cd11317  79 GVRVYVDAVINHMAG------------------------------------------------DANEVRNCELVGLADLN 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 185 LEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNwfPAGSKPFIYQEVIDLGGEPIKSSDYFG 264
Cdd:cd11317 111 TESDYVRDKIADYLNDLISLGVAGFRIDAAKHMWPEDLAAILARLKDLNGG--PLGSRPYIYQEVIDGGGEAIQPSEYTG 188

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 265 NGRVTEFKYGAKLGTVIRKWNGEKmsYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGaSILTFWDARLYKMAVGFML 344
Cdd:cd11317 189 NGDVTEFRYARGLSNAFRGKIKLL--LLKNFGEGWGLLPSERAVVFVDNHDNQRGHGGGG-DMLTYKDGRRYKLANAFML 265

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10280622 345 AHPYGFTRVMSSYRWPrqfqngndvNDWVGPPNN-NGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVV 416
Cdd:cd11317 266 AWPYGTPRVMSSYYFS---------DSDQGPPSDgSGNTLSVTINDDGTCGGGWVCEHRWPAIANMVGFRNAV 329
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 28-420 6.12e-50

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: 174.77  E-value: 6.12e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  28 IVHLFEWRWVDIALECERyLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRS-GNEDEFRNMVTRCNNVGV 106
Cdd:cd11315   4 ILHAFDWSFNTIKENLPE-IAAAGYTAIQTSPPQKSKEGGNEGGNWWYRYQPTDYRIGNNQlGTEDDFKALCAAAHKYGI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 107 RIYVDAVINHMsgnavsagTSSTCGSYFNPGSRDFPAVPYSGWDFNDGkcktgsgDIENYNDATQVRDCRLVGLLDLALE 186
Cdd:cd11315  83 KIIVDVVFNHM--------ANEGSAIEDLWYPSADIELFSPEDFHGNG-------GISNWNDRWQVTQGRLGGLPDLNTE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 187 KDYVRSKIAEYMNHLIDIGVAGFRLDASKHM-------WPGD-IKAILDKLHNLNsnwfpagskPFIYQEVIDLGGEPIK 258
Cdd:cd11315 148 NPAVQQQQKAYLKALVALGVDGFRFDAAKHIelpdepsKASDfWTNILNNLDKDG---------LFIYGEVLQDGGSRDS 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 259 S-SDYFGNGRVTEFKYGAKL-GTVIRKWNGEKMSYLKNWGEGwgfMPSDRALVFVDNHDNQrGHGAGGASILTFWDARly 336
Cdd:cd11315 219 DyASYLSLGGVTASAYGFPLrGALKNAFLFGGSLDPASYGQA---LPSDRAVTWVESHDTY-NNDGFESTGLDDEDER-- 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 337 kMAVGFMLAHPYGFTRVMSsyrwpRQFQNGNDvNDWVGPpnnngvikevtinpdttCGNDWVCEHrwrQIRNMVNFRNVV 416
Cdd:cd11315 293 -LAWAYLAARDGGTPLFFS-----RPNGSGGT-NPQIGD-----------------RGDDAWKSP---DVVAVNKFHNAM 345


                ....
gi 10280622 417 DGQP 420
Cdd:cd11315 346 HGQP 349
Aamy_C smart00632
Aamy_C domain;
422-510 2.21e-30

Aamy_C domain;


Pssm-ID: 214749  Cd Length: 81  Bit Score: 113.10  E-value: 2.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622    422 TNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISgdkinGNCTGIKIYVSDDGKAHFSISNSAEdp 501
Cdd:smart00632   1 TNWWDNGDNQIAFERGSKGFVAINRSDSDLTITLQTSLPAGTYCDVIS-----GLCTGKSVTVGSNGIATFTLPAGGA-- 73


                   ....*....
gi 10280622    502 fIAIHAESK 510
Cdd:smart00632  74 -VAIHVDAK 81
Aamy smart00642
Alpha-amylase domain;
28-120 8.65e-27

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 106.26  E-value: 8.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622     28 IVHLFEWR-------WVDIALECErYLAPKGFGGVQVSPPNENVaihnPFRPWWERYQPVSYKLC-TRSGNEDEFRNMVT 99
Cdd:smart00642   3 YPDRFADGngdgggdLQGIIEKLD-YLKDLGVTAIWLSPIFESP----QGYPSYHGYDISDYKQIdPRFGTMEDFKELVD 77

                           90       100
                   ....*....|....*....|.
gi 10280622    100 RCNNVGVRIYVDAVINHMSGN 120
Cdd:smart00642  78 AAHARGIKVILDVVINHTSDG 98
Alpha-amylase_C pfam02806
Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ...
 421-508 9.84e-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: 75.45  E-value: 9.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   421 FTNWYDNGSNQVAFGRGN---RGFIVFNNDDWTFSLTLQTGLP-AGTYCDVISGDKIN--GNCTGIKIYVSDDGKAHFSI 494
Cdd:pfam02806   1 WIDGDDAENNVIAFERGDdggKLLVVFNFTPSVSYTDYRTGLPeAGTYCEVLNTDDEEygGSNTGEVVTVDGPGHPNSLT 80

                          90
                  ....*....|....
gi 10280622   495 SNSAEDPFIAIHAE 508
Cdd:pfam02806  81 LTLPPLSALVLKVE 94
AmyAc_family cd00551
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 45-347 1.67e-16

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


Pssm-ID: 200451 [Multi-domain]  Cd Length: 260  Bit Score: 79.52  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  45 RYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYqpvSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHmsgnavsa 124
Cdd:cd00551  32 DYLKDLGVTAIWLTPIFESPEYDGYDKDDGYLD---YYEIDPRLGTEEDFKELVKAAHKRGIKVILDLVFNH-------- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 125 gtsstcgsyfnpgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrlvglldlalekdyvrskiaEYMNHLIDI 204
Cdd:cd00551 101 -----------------------------------------------------------------------DILRFWLDE 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 205 GVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPagsKPFIYQEVIDlGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKW 284
Cdd:cd00551 110 GVDGFRLDAAKHVPKPEPVEFLREIRKDAKLAKP---DTLLLGEAWG-GPDELLAKAGFDDGLDSVFDFPLLEALRDALK 185

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10280622 285 NGEKMSYLKNWGEgWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLyKMAVGFMLAHP 347
Cdd:cd00551 186 GGEGALAILAALL-LLNPEGALLVNFLGNHDTFRLADLVSYKIVELRKARL-KLALALLLTLP 246
Alpha-amylase pfam00128
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ...
 82-344 1.71e-14

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: 74.70  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622    82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSgnavsagtssTCGSYFNPgSRDFPAVPYS-GWDFNDGKCKTGS 160
Cdd:pfam00128  42 YKIDPHYGTMEDFKELISKAHERGIKVILDLVVNHTS----------DEHAWFQE-SRSSKDNPYRdYYFWRPGGGPIPP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   161 GDIENYNDATQVRDCR----------LVGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLH 230
Cdd:pfam00128 111 NNWRSYFGGSAWTYDEkgqeyylhlfVAGQPDLNWENPEVRNELYDVVRFWLDKGIDGFRIDVVKHISKVPGLPFENNGP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   231 NLNSNWFPAGSKPFIYQEVIDLG------GEPIKSSDYFGNGRVTE----FKYGAKLGTVIrKWNGEKMSY--LKNWGEG 298
Cdd:pfam00128 191 FWHEFTQAMNETVFGYKDVMTVGevfhgdGEWARVYTTEARMELEMgfnfPHNDVALKPFI-KWDLAPISArkLKEMITD 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 10280622   299 W-GFMP--SDRALVFVDNHDNQRghgaggasILTFW--DARLYKMAVGFML 344
Cdd:pfam00128 270 WlDALPdtNGWNFTFLGNHDQPR--------FLSRFgdDRASAKLLAVFLL 312
AmyAc_AmyMalt_CGTase_like cd11320
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ...
 46-344 2.04e-14

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: 75.02  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  46 YLAPKGFGGVQVSPPNENV------AIHNPFRPWWER-YqpvsYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHmS 118
Cdd:cd11320  55 YLKDLGVTAIWISPPVENInspiegGGNTGYHGYWARdF----KRTNEHFGTWEDFDELVDAAHANGIKVIIDFVPNH-S 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 119 GNAVSAGTsstcGSYFNPGS--RDFPAVPySGWdFNdgkcktGSGDIENYNDATQVRDCRLVGLLDLALEKDYVRSKIAE 196
Cdd:cd11320 130 SPADYAED----GALYDNGTlvGDYPNDD-NGW-FH------HNGGIDDWSDREQVRYKNLFDLADLNQSNPWVDQYLKD 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 197 YMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSnwfpagskPFIYQEVIDLGGEPiKSSDY--FGNGR---VTEF 271
Cdd:cd11320 198 AIKFWLDHGIDGIRVDAVKHMPPGWQKSFADAIYSKKP--------VFTFGEWFLGSPDP-GYEDYvkFANNSgmsLLDF 268

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10280622 272 KYGAKLGTVIRKwNGEKMSYLKNWGEGWG--FMPSDRALVFVDNHDNQRGHGAGGasiltfwDARLYKMAVGFML 344
Cdd:cd11320 269 PLNQAIRDVFAG-FTATMYDLDAMLQQTSsdYNYENDLVTFIDNHDMPRFLTLNN-------NDKRLHQALAFLL 335
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 82-224 1.50e-13

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: 72.21  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAVSAGTSStcgSYFNPgsrdfpavpysgwdFNDGK-----C 156
Cdd:cd11319  88 YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHMASAGPGSDVDY---SSFVP--------------FNDSSyyhpyC 150

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10280622 157 ktgsgDIENYNDATQVRDCRL----VGLLDLALEKDYVRSKIAEYMNHLI-DIGVAGFRLDASKHM----WPGDIKA 224
Cdd:cd11319 151 -----WITDYNNQTSVEDCWLgddvVALPDLNTENPFVVSTLNDWIKNLVsNYSIDGLRIDTAKHVrkdfWPGFVEA 222
AmyA COG0366
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism];
89-347 1.69e-12

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


Pssm-ID: 440135 [Multi-domain]  Cd Length: 413  Bit Score: 69.12  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMS------GNAVSAGTSSTcgsyfnpgsRDFpavpYSGWDFNDGKCKTGSGD 162
Cdd:COG0366  76 GTLADFDELVAEAHARGIKVILDLVLNHTSdehpwfQEARAGPDSPY---------RDW----YVWRDGKPDLPPNNWFS 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 163 IENYNDATQVRDCR-------LVGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMW-----PGDIKAILDKLH 230
Cdd:COG0366 143 IFGGSAWTWDPEDGqyylhlfFSSQPDLNWENPEVREELLDVLRFWLDRGVDGFRLDAVNHLDkdeglPENLPEVHEFLR 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 231 NLNSNWFPAGSKPFIYQEVIdlGGEPIKSSDYFGNGR---VTEFKYGAKLGTVIRKWNGEKM-SYLKNWGEGwgfMPSDR 306
Cdd:COG0366 223 ELRAAVDEYYPDFFLVGEAW--VDPPEDVARYFGGDEldmAFNFPLMPALWDALAPEDAAELrDALAQTPAL---YPEGG 297

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 10280622 307 ALV-FVDNHDNQRghgaggasILTFW----DARLYKMAVGFMLAHP 347
Cdd:COG0366 298 WWAnFLRNHDQPR--------LASRLggdyDRRRAKLAAALLLTLP 335
AmyAc_bac2_AmyA cd11316
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 89-348 4.30e-07

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


Pssm-ID: 200455 [Multi-domain]  Cd Length: 403  Bit Score: 52.20  E-value: 4.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNA---VSAGTSSTCG--SYFNpgsrdFPAVPYSGWDFNDGKCKTGSGDI 163
Cdd:cd11316  67 GTMEDFERLIAEAHKRGIKVIIDLVINHTSSEHpwfQEAASSPDSPyrDYYI-----WADDDPGGWSSWGGNVWHKAGDG 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 164 ENYNDA-TQvrdcrlvGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDiKAILDKLHNLNS-NWFPA-- 239
Cdd:cd11316 142 GYYYGAfWS-------GMPDLNLDNPAVREEIKKIAKFWLDKGVDGFRLDAAKHIYENG-EGQADQEENIEFwKEFRDyv 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 240 -GSKP--FIYQEVIDLGGEPiksSDYFGNG--RVTEFKYGAKLGTVIRKWNG--EKMSYLKNW-GEGWGFMPSDRALVFV 311
Cdd:cd11316 214 kSVKPdaYLVGEVWDDPSTI---APYYASGldSAFNFDLAEAIIDSVKNGGSgaGLAKALLRVyELYAKYNPDYIDAPFL 290

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 10280622 312 DNHDNQRGHGAGGAsiltfwDARLYKMAVGFML---AHPY 348
Cdd:cd11316 291 SNHDQDRVASQLGG------DEAKAKLAAALLLtlpGNPF 324
PLN02784 PLN02784
alpha-amylase
 21-332 8.08e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 51.94  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   21 TQQGRTSIVHLFEW------RWVDIALECERYLAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTRSGNEDE 93
Cdd:PLN02784 498 TGSGFEILCQGFNWeshksgRWYMELGEKAAELSSLGFTVVWLPPPTESVS------P--EGYMPKDlYNLNSRYGTIDE 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   94 FRNMVTRCNNVGVRIYVDAVINHMSGNAVSA-GTSSTCGSYFNPGSRdfpAVPYSGWDFNdGKCKTGSGDieNYNDATQV 172
Cdd:PLN02784 570 LKDLVKSFHEVGIKVLGDAVLNHRCAHFQNQnGVWNIFGGRLNWDDR---AVVADDPHFQ-GRGNKSSGD--NFHAAPNI 643

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  173 RDcrlvglldlalEKDYVRSKIAEYMNHLID-IGVAGFRLDASKHMWPGDIKAILDKlhnlNSNWFPAG----SKPFIY- 246
Cdd:PLN02784 644 DH-----------SQDFVRKDLKEWLCWMRKeVGYDGWRLDFVRGFWGGYVKDYMEA----SEPYFAVGeywdSLSYTYg 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  247 ----------QEVIDLggepIKSSdyfgNGRVTEFKYGAK--LGTVIRKWNGEKMSYLKNWGEG-WGFMPSdRALVFVDN 313
Cdd:PLN02784 709 emdynqdahrQRIVDW----INAT----NGTAGAFDVTTKgiLHSALERCEYWRLSDQKGKPPGvVGWWPS-RAVTFIEN 779

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 10280622  314 HD--NQRGHG--------AGGASILT-------FWD 332
Cdd:PLN02784 780 HDtgSTQGHWrfpegkemQGYAYILThpgtpavFYD 815
AmyAc_bac_CMD_like cd11354
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 82-213 1.48e-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: 200491 [Multi-domain]  Cd Length: 357  Bit Score: 50.40  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  82 YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGN--AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDfndgkcktG 159
Cdd:cd11354  67 YRIDPRLGDDEDFDALIAAAHERGLRVLLDGVFNHVGRShpAVAQALEDGPGSEEDRWHGHAGGGTPAVFE--------G 138

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 10280622 160 SGDienyndatqvrdcrlvgLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDA 213
Cdd:cd11354 139 HED-----------------LVELDHSDPAVVDMVVDVMCHWLDRGIDGWRLDA 175
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 47-227 1.05e-05

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: 47.22  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  47 LAPKGFGGVQVSPPNENVAIHNpfrpwwERYQPVS-YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNavSAG 125
Cdd:cd11314  27 LAAAGFTAIWLPPPSKSVSGSS------MGYDPGDlYDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRSGP--DTG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 126 TsstcgsyfnpgsrDFPAVPysgwdfndgkcktgsgDIENYNdatqvrdcrlvglldlalekDYVRSKIAEYMNHLI-DI 204
Cdd:cd11314  99 E-------------DFGGAP----------------DLDHTN--------------------PEVQNDLKAWLNWLKnDI 129

                       170       180
                ....*....|....*....|...
gi 10280622 205 GVAGFRLDASKHMWPGDIKAILD 227
Cdd:cd11314 130 GFDGWRFDFVKGYAPSYVKEYNE 152
AmyAc_bac_CMD_like_2 cd11339
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ...
 182-351 1.17e-04

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


Pssm-ID: 200478 [Multi-domain]  Cd Length: 344  Bit Score: 44.17  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 182 DLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHM----WPGDIKAILDKLHnlnsnwfpagsKP--FIYQEVIDlgGE 255
Cdd:cd11339 126 DLNTENPEVVDYLIDAYKWWIDTGVDGFRIDTVKHVprefWQEFAPAIRQAAG-----------KPdfFMFGEVYD--GD 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 256 PIKSSDYF---GNGRVTEFKYGAKLGTVIRkwNGEKMSYLKNW-GEGWGFMPSDRALVFVDNHDNQRghgaggasILTFW 331
Cdd:cd11339 193 PSYIAPYTttaGGDSVLDFPLYGAIRDAFA--GGGSGDLLQDLfLSDDLYNDATELVTFLDNHDMGR--------FLSSL 262

                       170       180
                ....*....|....*....|
gi 10280622 332 DARLYKMAVGFMLAHPYGFT 351
Cdd:cd11339 263 KDGSADGTARLALALALLFT 282
AmyAc_maltase-like cd11329
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ...
 89-216 1.30e-03

Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200468 [Multi-domain]  Cd Length: 477  Bit Score: 41.21  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  89 GNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAV----SAGTSSTCGSYF--NPGSRDFPAVPY------SGWDFNDGKC 156
Cdd:cd11329 112 GVESDLKELVKTAKQKDIKVILDLTPNHSSKQHPlfkdSVLKEPPYRSAFvwADGKGHTPPNNWlsvtggSAWKWVEDRQ 191

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622 157 KTGSgdienYNDATQVrdcrlvgllDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKH 216
Cdd:cd11329 192 YYLH-----QFGPDQP---------DLNLNNPAVVDELKDVLKHWLDLGVRGFRLANAKY 237
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 86-217 2.13e-03

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 40.64  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   86 TRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSG------------------NAVSAGTSSTCGSYFN-PG----SRDFP 142
Cdd:PRK09441  75 TKYGTKEELLNAIDALHENGIKVYADVVLNHKAGadeketfrvvevdpddrtQIISEPYEIEGWTRFTfPGrggkYSDFK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  143 AVPY--SGWDFNDGKCKTGSGDIENYND--ATQVRDCR-----LVGlLDLALEKDYVRSKIAEYMNHLID-IGVAGFRLD 212
Cdd:PRK09441 155 WHWYhfSGTDYDENPDESGIFKIVGDGKgwDDQVDDENgnfdyLMG-ADIDFRHPEVREELKYWAKWYMEtTGFDGFRLD 233


                 ....*
gi 10280622  213 ASKHM 217
Cdd:PRK09441 234 AVKHI 238
PLN02447 PLN02447
1,4-alpha-glucan-branching enzyme
 85-155 4.20e-03

1,4-alpha-glucan-branching enzyme


Pssm-ID: 215246 [Multi-domain]  Cd Length: 758  Bit Score: 39.66  E-value: 4.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10280622   85 CTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMSGNAVS--AGTSSTCGSYFNPGSRDFPAVpysgWD---FNDGK 155
Cdd:PLN02447 293 SSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASKNTLDglNGFDGTDGSYFHSGPRGYHWL----WDsrlFNYGN 364
PLN02361 PLN02361
alpha-amylase
 47-227 9.55e-03

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 38.26  E-value: 9.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622   47 LAPKGFGGVQVSPPNENVAihnpfrPwwERYQPVS-YKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHmsgnavSAG 125
Cdd:PLN02361  38 LAKSGFTSAWLPPPSQSLA------P--EGYLPQNlYSLNSAYGSEHLLKSLLRKMKQYNVRAMADIVINH------RVG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10280622  126 TSSTCGSYFNpgsrDFPAVPYSgWDFNDGKCKTG------SGDIENyndatqvrdcrlvGLLDLALEKDYVRSKIAEYMN 199
Cdd:PLN02361 104 TTQGHGGMYN----RYDGIPLP-WDEHAVTSCTGglgnrsTGDNFN-------------GVPNIDHTQHFVRKDIIGWLI 165

                        170       180
                 ....*....|....*....|....*....
gi 10280622  200 HLI-DIGVAGFRLDASKHMWPGDIKAILD 227
Cdd:PLN02361 166 WLRnDVGFQDFRFDFAKGYSAKFVKEYIE 194
 
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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