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Conserved domains on  [gi|24583253|ref|NP_609354|]
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uncharacterized protein Dmel_CG5731 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmyAc_family super family cl38930
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
25-308 0e+00

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.


The actual alignment was detected with superfamily member pfam16499:

Pssm-ID: 476817 [Multi-domain]  Cd Length: 284  Bit Score: 505.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253    25 TPPMGWLSWERFRCNTDCVNDPDNCISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRKRFPNGIK 104
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   105 ALSDYIHSRGLKFGIYEDYGNYTCAGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGYSTFGRLLNSTGKSMV 184
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCYSNLEDLVEGYPNMSFALNKTGRPIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   185 YSCSWPVYQIYAGIQPNYSAIQTHCNLWRNYDDIQDSWASVENIIDYYGNNQDVIAPNAGPGHWNDPDMLIIGNFGLSYE 264
Cdd:pfam16499 161 YSCEWPLYMGGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSYD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 24583253   265 QAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQD 308
Cdd:pfam16499 241 QQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
Melibiase_2_C super family cl29048
Alpha galactosidase A C-terminal beta sandwich domain;
311-399 4.26e-15

Alpha galactosidase A C-terminal beta sandwich domain;


The actual alignment was detected with superfamily member pfam17450:

Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 70.07  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   311 GIQGRRIYKHKGIEIWSRPIGPLyqnfySYAIAFVNRRTDGTPS--DISVTLKELGLINFSGYRVEDLYENVDYGVLYPN 388
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDN-----SLAVAVLNRREIGMPYryTLSLAKLGYGKVCSPACNVTDIFPGKKLGVFELT 75
                          90
                  ....*....|.
gi 24583253   389 TKIKVKVNPSG 399
Cdd:pfam17450  76 SNLVVSVNPTG 86
 
Name Accession Description Interval E-value
Melibiase_2 pfam16499
Alpha galactosidase A;
25-308 0e+00

Alpha galactosidase A;


Pssm-ID: 374582 [Multi-domain]  Cd Length: 284  Bit Score: 505.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253    25 TPPMGWLSWERFRCNTDCVNDPDNCISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRKRFPNGIK 104
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   105 ALSDYIHSRGLKFGIYEDYGNYTCAGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGYSTFGRLLNSTGKSMV 184
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCYSNLEDLVEGYPNMSFALNKTGRPIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   185 YSCSWPVYQIYAGIQPNYSAIQTHCNLWRNYDDIQDSWASVENIIDYYGNNQDVIAPNAGPGHWNDPDMLIIGNFGLSYE 264
Cdd:pfam16499 161 YSCEWPLYMGGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSYD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 24583253   265 QAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQD 308
Cdd:pfam16499 241 QQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
GH27 cd14792
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
26-308 5.69e-137

glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269893 [Multi-domain]  Cd Length: 271  Bit Score: 392.69  E-value: 5.69e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  26 PPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRKRFPNGIKA 105
Cdd:cd14792   1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 106 LSDYIHSRGLKFGIYEDYGNYTCA--GYPGIIGYEEKDALQFADWNVDYVKLDGCYA--LPYDMDHGYSTFGRLLNSTGK 181
Cdd:cd14792  71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGApsGRLDAQERYTAMSDALNATGR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 182 SMVYSCSWPVYQIYAGiqpnysAIQTHCNLWRNYDDIQDSWASVENIIDYYGNNQDViAPNAGPGHWNDPDMLIIGNFGL 261
Cdd:cd14792 151 PIVLSLSWWGYPDPWG------WAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEY-AAPAGPGHWNDPDMLEVGNGGL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 24583253 262 -SYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQD 308
Cdd:cd14792 224 gTDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
PLN02229 PLN02229
alpha-galactosidase
11-381 5.46e-101

alpha-galactosidase


Pssm-ID: 177874 [Multi-domain]  Cd Length: 427  Bit Score: 306.86  E-value: 5.46e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   11 SSTFGKC-LDNGLAKTPPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHD 89
Cdd:PLN02229  47 TSMYGRLqLNNGLARTPQMGWNSWNFFACN----------INETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   90 GKLVADRKRFPNGIKALSDYIHSRGLKFGIYEDYGNYTCAGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGY 169
Cdd:PLN02229 117 GQLVPDPKTFPSGIKLLADYVHSKGLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCYNLGIKPIERY 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  170 STFGRLLNSTGKSMVYS-CSWPVYQ--IYAGiqpnysaiqTHCNLWRNYDDIQDSWASVENIIDYygNNQdvIAPNAGPG 246
Cdd:PLN02229 197 PPMRDALNATGRSIFYSlCEWGVDDpaLWAG---------KVGNSWRTTDDINDTWASMTTIADL--NNK--WAAYAGPG 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  247 HWNDPDMLIIGNFGLSYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQDPLGIQGRRIY---KHKGI 323
Cdd:PLN02229 264 GWNDPDMLEVGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQangKNGCQ 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24583253  324 EIWSrpiGPLYQNfySYAIAFVNRRTDgtPSDISVTLKELGLINFSGYRVEDLYENVD 381
Cdd:PLN02229 344 QVWA---GPLSGD--RLVVALWNRCSE--PATITASWDVIGLESSISVSVRDLWKHKD 394
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
20-180 4.26e-16

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 76.94  E-value: 4.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  20 NGLAKTPPMGWLSWERFRCNtdcvndpdncISEQLFQTMtdivvADGYASVGYEYINIDDCWlEKHRSHD----GKLVAD 95
Cdd:COG3345  28 GPPDKPRPVGWNSWEAYYFD----------FTEEKLLAL-----ADAAAELGVELFVLDDGW-FGGRRDDtaglGDWLVD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  96 RKRFPNGIKALSDYIHSRGLKFGI-YEdygnytcagyPGIIGYEEKDALQFADWNV---DYVKLDGCYALPYDM------ 165
Cdd:COG3345  92 PEKFPNGLKPLADRIHALGMKFGLwVE----------PEMVNPDSDLYREHPDWVLkdpDGEPVEGRNQYVLDLsnpevr 161
                       170
                ....*....|....*
gi 24583253 166 DHGYSTFGRLLNSTG 180
Cdd:COG3345 162 DYLFEVLDRLLAEWG 176
Melibiase_2_C pfam17450
Alpha galactosidase A C-terminal beta sandwich domain;
311-399 4.26e-15

Alpha galactosidase A C-terminal beta sandwich domain;


Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 70.07  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   311 GIQGRRIYKHKGIEIWSRPIGPLyqnfySYAIAFVNRRTDGTPS--DISVTLKELGLINFSGYRVEDLYENVDYGVLYPN 388
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDN-----SLAVAVLNRREIGMPYryTLSLAKLGYGKVCSPACNVTDIFPGKKLGVFELT 75
                          90
                  ....*....|.
gi 24583253   389 TKIKVKVNPSG 399
Cdd:pfam17450  76 SNLVVSVNPTG 86
 
Name Accession Description Interval E-value
Melibiase_2 pfam16499
Alpha galactosidase A;
25-308 0e+00

Alpha galactosidase A;


Pssm-ID: 374582 [Multi-domain]  Cd Length: 284  Bit Score: 505.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253    25 TPPMGWLSWERFRCNTDCVNDPDNCISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRKRFPNGIK 104
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   105 ALSDYIHSRGLKFGIYEDYGNYTCAGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGYSTFGRLLNSTGKSMV 184
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCYSNLEDLVEGYPNMSFALNKTGRPIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   185 YSCSWPVYQIYAGIQPNYSAIQTHCNLWRNYDDIQDSWASVENIIDYYGNNQDVIAPNAGPGHWNDPDMLIIGNFGLSYE 264
Cdd:pfam16499 161 YSCEWPLYMGGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSYD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 24583253   265 QAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQD 308
Cdd:pfam16499 241 QQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
GH27 cd14792
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
26-308 5.69e-137

glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269893 [Multi-domain]  Cd Length: 271  Bit Score: 392.69  E-value: 5.69e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  26 PPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRKRFPNGIKA 105
Cdd:cd14792   1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 106 LSDYIHSRGLKFGIYEDYGNYTCA--GYPGIIGYEEKDALQFADWNVDYVKLDGCYA--LPYDMDHGYSTFGRLLNSTGK 181
Cdd:cd14792  71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGApsGRLDAQERYTAMSDALNATGR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 182 SMVYSCSWPVYQIYAGiqpnysAIQTHCNLWRNYDDIQDSWASVENIIDYYGNNQDViAPNAGPGHWNDPDMLIIGNFGL 261
Cdd:cd14792 151 PIVLSLSWWGYPDPWG------WAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEY-AAPAGPGHWNDPDMLEVGNGGL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 24583253 262 -SYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQD 308
Cdd:cd14792 224 gTDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
PLN02229 PLN02229
alpha-galactosidase
11-381 5.46e-101

alpha-galactosidase


Pssm-ID: 177874 [Multi-domain]  Cd Length: 427  Bit Score: 306.86  E-value: 5.46e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   11 SSTFGKC-LDNGLAKTPPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHD 89
Cdd:PLN02229  47 TSMYGRLqLNNGLARTPQMGWNSWNFFACN----------INETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   90 GKLVADRKRFPNGIKALSDYIHSRGLKFGIYEDYGNYTCAGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGY 169
Cdd:PLN02229 117 GQLVPDPKTFPSGIKLLADYVHSKGLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCYNLGIKPIERY 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  170 STFGRLLNSTGKSMVYS-CSWPVYQ--IYAGiqpnysaiqTHCNLWRNYDDIQDSWASVENIIDYygNNQdvIAPNAGPG 246
Cdd:PLN02229 197 PPMRDALNATGRSIFYSlCEWGVDDpaLWAG---------KVGNSWRTTDDINDTWASMTTIADL--NNK--WAAYAGPG 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  247 HWNDPDMLIIGNFGLSYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQDPLGIQGRRIY---KHKGI 323
Cdd:PLN02229 264 GWNDPDMLEVGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQangKNGCQ 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24583253  324 EIWSrpiGPLYQNfySYAIAFVNRRTDgtPSDISVTLKELGLINFSGYRVEDLYENVD 381
Cdd:PLN02229 344 QVWA---GPLSGD--RLVVALWNRCSE--PATITASWDVIGLESSISVSVRDLWKHKD 394
PLN02808 PLN02808
alpha-galactosidase
18-379 1.35e-97

alpha-galactosidase


Pssm-ID: 166449 [Multi-domain]  Cd Length: 386  Bit Score: 296.87  E-value: 1.35e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   18 LDNGLAKTPPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRK 97
Cdd:PLN02808  24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   98 RFPNGIKALSDYIHSRGLKFGIYEDYGNYTCAG-YPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGYSTFGRLL 176
Cdd:PLN02808  94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSPQERYPKMSKAL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  177 NSTGKSMVYS-CSWpvyqiyaGIQPNYSAIQTHCNLWRNYDDIQDSWASVENIIDyygnNQDVIAPNAGPGHWNDPDMLI 255
Cdd:PLN02808 174 LNSGRPIFFSlCEW-------GQEDPATWAGDIGNSWRTTGDIQDNWDSMTSRAD----QNDRWASYARPGGWNDPDMLE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  256 IGNFGLSYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQDPLGIQGRRIYKHKGIEIWSrpiGPLYQ 335
Cdd:PLN02808 243 VGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWA---GPLSK 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 24583253  336 NfySYAIAFVNRRTdgTPSDISVTLKELGLINFSGYRVEDLYEN 379
Cdd:PLN02808 320 K--RVAVVLWNRGS--SRATITARWSDIGLNSSAVVNARDLWAH 359
PLN02692 PLN02692
alpha-galactosidase
18-379 6.27e-91

alpha-galactosidase


Pssm-ID: 178295 [Multi-domain]  Cd Length: 412  Bit Score: 280.39  E-value: 6.27e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   18 LDNGLAKTPPMGWLSWERFRCNTDcvndpdncisEQLFQTMTDIVVADGYASVGYEYINIDDCWLEKHRSHDGKLVADRK 97
Cdd:PLN02692  48 LANGLGITPPMGWNSWNHFSCKID----------EKMIKETADALVSTGLSKLGYTYVNIDDCWAEIARDEKGNLVPKKS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   98 RFPNGIKALSDYIHSRGLKFGIYEDYGNYTCAG-YPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDHGYSTFGRLL 176
Cdd:PLN02692 118 TFPSGIKALADYVHSKGLKLGIYSDAGYFTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCNNDGSKPTVRYPVMTRAL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  177 NSTGKSMVYS-CSWpvyqiyAGIQPNYSAIQTHcNLWRNYDDIQDSWASVENIIDYygnnQDVIAPNAGPGHWNDPDMLI 255
Cdd:PLN02692 198 MKAGRPIFFSlCEW------GDMHPALWGSKVG-NSWRTTNDISDTWDSMISRADM----NEVYAELARPGGWNDPDMLE 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  256 IGNFGLSYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQDPLGIQGRRIYKHKGIEIWSrpiGPLyq 335
Cdd:PLN02692 267 VGNGGMTKDEYIVHFSIWAISKAPLLLGCDVRNMTKETMDIVANKEVIAVNQDPLGVQAKKVRMEGDLEIWA---GPL-- 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 24583253  336 NFYSYAIAFVNRrtdgTPSDISVTL--KELGLINFSGYRVEDLYEN 379
Cdd:PLN02692 342 SGYRVALLLLNR----GPWRNSITAnwDDIGIPANSIVEARDLWEH 383
GH_D cd14790
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
26-303 2.53e-55

Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.


Pssm-ID: 269891 [Multi-domain]  Cd Length: 253  Bit Score: 183.21  E-value: 2.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  26 PPMGWLSWERFRcntdcvndpdNCISEQLFQTMTDIVVADGYasvGYEYINIDDCWLEKHRshDGKLVADRKRFPNGiKA 105
Cdd:cd14790   1 PPMGWLTWERYR----------QDIDEMLFMEMADRIAEDEL---PYKVFNIDDCWAKKDA--EGDFVPDPERFPRG-EA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 106 LSDYIHSRGLKFGIYedygnytcaGYPGIIGYEEKDALQFADWNVDYVKLDGCYALPYDMDH------------GYSTFG 173
Cdd:cd14790  65 MARRLHARGLKLGIW---------GDPFRLDWVEDDLQTLAEWGVDMFKLDFGESSGTPVQWfpqkmpnkeqaqGYEQMA 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 174 RLLNSTGKSMVYSCSWPVYQIYAGIqpnysaiqthCNLWRNYDDIQDSWASVENIIDYYGNNQDVIApnAGPGHWNDPDM 253
Cdd:cd14790 136 RALNATGEPIVYSGSWSAYQGGGEI----------CNLWRNYDDIQDSWDAVLSIVDWFFTNQDVLQ--AGGFHFNDPDM 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 24583253 254 LIIGNFGLSYEQAKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKII 303
Cdd:cd14790 204 LIIGNFGLSAEQSRSQMALWTIMDAPLLMSTDLSTISPSDKKILVNRLMI 253
PLN02899 PLN02899
alpha-galactosidase
2-289 1.69e-18

alpha-galactosidase


Pssm-ID: 178487 [Multi-domain]  Cd Length: 633  Bit Score: 87.54  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253    2 LATLWIILLSSTFGKCLDNGLAKTPPMGWLSWERFrCNTdcvndpdncISEQLFQTMTDIVvADGYASVGYEYINIDDCW 81
Cdd:PLN02899   7 FILFCLLSLSLWIGASSQQQLASFPPRGWNSYDSF-SWI---------VSEEEFLQNAEIV-SQRLLPFGYEYVVVDYLW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   82 LEKHR--------SHD-----GKLVADRKRFPN-----GIKALSDYIHSRGLKFGI------------------------ 119
Cdd:PLN02899  76 YRKKVegayvdslGFDvidewGRPIPDPGRWPSsrggkGFTEVAEKVHAMGLKFGIhvmrgistqavnantpildavkgg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  120 -YEDYG-----------NYTCAGYP-GIIGYEEK--------DAL--QFADWNVDYVKLDGCYALPYDMDHgYSTFGRLL 176
Cdd:PLN02899 156 aYEESGrqwrakdialkERACAWMShGFMSVNTKlgagkaflRSLydQYAEWGVDFVKHDCVFGDDFDLEE-ITYVSEVL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  177 NSTGKSMVYSCSwPVYQIYAGIQPNYSAiqtHCNLWRNYDDIQDSWASVE---NIIDYYGNNQDVIAPNAGPGHWNDPDM 253
Cdd:PLN02899 235 KELDRPIVYSLS-PGTSATPTMAKEVSG---LVNMYRITGDDWDTWGDVAahfDVSRDFAAAGLIGAKGLRGRSWPDLDM 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 24583253  254 LIIG-------NFG------LSYEQAKTQFAIWSILAAPLLMSVDLRTI 289
Cdd:PLN02899 311 LPLGwltdpgsNVGphracnLTLDEQKTQMTLWAMAKSPLMYGGDLRKL 359
PLN03231 PLN03231
putative alpha-galactosidase; Provisional
26-311 4.14e-16

putative alpha-galactosidase; Provisional


Pssm-ID: 178770 [Multi-domain]  Cd Length: 357  Bit Score: 79.25  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   26 PPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVvADGYASVGYEYINIDDCWLEKHR-----------SHD----- 89
Cdd:PLN03231   1 PPRGWNSYDSFSFT----------ISEEQFLENAKIV-SETLKPHGYEYVVIDYLWYRKLKhgwfktsakspGYDlidkw 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   90 GKLVADRKRFPN-----GIKALSDYIHSRGLKFGIYEDYGNYTCA--------GYPGIIGY--EEKD-AL---------- 143
Cdd:PLN03231  70 GRPLPDPKRWPSttggkGFAPIAAKVHALGLKLGIHVMRGISTTAvkkktpilGAFKSNGHawNAKDiALmdqacpwmqq 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  144 ---------------------QFADWNVDYVKLDGCYALPYDMDHGYSTFGRLLNSTGKSMVYSCSwPVYQIYAGIQpny 202
Cdd:PLN03231 150 cfvgvntsseggklfiqslydQYASWGIDFIKHDCVFGAENPQLDEILTVSKAIRNSGRPMIYSLS-PGDGATPGLA--- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  203 SAIQTHCNLWRNYDDIQDSWASVE---NIIDYYGNNQDVIAPNAGPGH-WNDPDMLIIG-------------NFGLSYEQ 265
Cdd:PLN03231 226 ARVAQLVNMYRVTGDDWDDWKYLVkhfDVARDFAAAGLIAIPSVVGGKsWVDLDMLPFGrltdpaaaygpyrNSRLSLEE 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 24583253  266 AKTQFAIWSILAAPLLMSVDLRTIRPQFKHILQNRKIIAVDQDPLG 311
Cdd:PLN03231 306 KKTQMTLWAVAKSPLMFGGDLRRLDNETLSLLTNPTVLEVNSHSTG 351
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
20-180 4.26e-16

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 76.94  E-value: 4.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  20 NGLAKTPPMGWLSWERFRCNtdcvndpdncISEQLFQTMtdivvADGYASVGYEYINIDDCWlEKHRSHD----GKLVAD 95
Cdd:COG3345  28 GPPDKPRPVGWNSWEAYYFD----------FTEEKLLAL-----ADAAAELGVELFVLDDGW-FGGRRDDtaglGDWLVD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  96 RKRFPNGIKALSDYIHSRGLKFGI-YEdygnytcagyPGIIGYEEKDALQFADWNV---DYVKLDGCYALPYDM------ 165
Cdd:COG3345  92 PEKFPNGLKPLADRIHALGMKFGLwVE----------PEMVNPDSDLYREHPDWVLkdpDGEPVEGRNQYVLDLsnpevr 161
                       170
                ....*....|....*
gi 24583253 166 DHGYSTFGRLLNSTG 180
Cdd:COG3345 162 DYLFEVLDRLLAEWG 176
Melibiase_2_C pfam17450
Alpha galactosidase A C-terminal beta sandwich domain;
311-399 4.26e-15

Alpha galactosidase A C-terminal beta sandwich domain;


Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 70.07  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   311 GIQGRRIYKHKGIEIWSRPIGPLyqnfySYAIAFVNRRTDGTPS--DISVTLKELGLINFSGYRVEDLYENVDYGVLYPN 388
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDN-----SLAVAVLNRREIGMPYryTLSLAKLGYGKVCSPACNVTDIFPGKKLGVFELT 75
                          90
                  ....*....|.
gi 24583253   389 TKIKVKVNPSG 399
Cdd:pfam17450  76 SNLVVSVNPTG 86
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
26-161 2.45e-12

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 67.25  E-value: 2.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253  26 PPMGWLSWERFRCNtdcvndpdncISEQLFQTMTDIVvadgyASVGYEYINIDDCWlEKHRSHDGKLV----ADRKRFPN 101
Cdd:cd14791   2 RPVGWNSWYAYYFD----------ITEEKLLELADAA-----AELGVELFVIDDGW-FGARNDDYAGLgdwlVDPEKFPD 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253 102 GIKALSDYIHSRGLKFGI-----------------------YEDYGNYT-------CAGYPGIIGYEEKDALQF-ADWNV 150
Cdd:cd14791  66 GLKALADRIHALGMKFGLwlepemvgpdselyrehpdwllkDPGGPPVTgrnqyvlDLSNPEVRDYLREVIDRLlREWGI 145
                       170
                ....*....|.
gi 24583253 151 DYVKLDGCYAL 161
Cdd:cd14791 146 DYLKWDFNRAG 156
Melibiase_C pfam17801
Alpha galactosidase C-terminal beta sandwich domain; This domain is found at the C-terminus of ...
322-404 1.11e-09

Alpha galactosidase C-terminal beta sandwich domain; This domain is found at the C-terminus of alpha galactosidase enzymes.


Pssm-ID: 465512 [Multi-domain]  Cd Length: 74  Bit Score: 54.57  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253   322 GIEIWSrpiGPLYQNfySYAIAFVNRrtdGTPSDISVTLKELGLINFSGYRVEDLYENVDYGvlypNTKIKVKVNPSGVV 401
Cdd:pfam17801   3 DLQVWA---KPLSNG--DVAVALFNR---GGPSTVTVDLSDLGLPGASSYSVRDLWTGKDLG----TGSTSATVPPHGVA 70

                  ...
gi 24583253   402 MLK 404
Cdd:pfam17801  71 LLR 73
Melibiase pfam02065
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
63-184 3.65e-07

Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.


Pssm-ID: 307952  Cd Length: 347  Bit Score: 51.63  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583253    63 VADGYASVGYEYINIDDCWLEKHRSHDGKL---VADRKRFPNGIKALSDYIHSRGLKFGIYEDygnytcagyPGIIGYEE 139
Cdd:pfam02065  63 LADEAADLGIELFVLDDGWFGHRNDDNSSLgdwFVNPRKFPNGLDPLAKQVHALGMQFGLWFE---------PEMVNPNS 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24583253   140 KDALQFADWNVDYVK-----------LDgcYALPYDMDHGYSTFGRLLNSTGKSMV 184
Cdd:pfam02065 134 DLYRQHPDWVLHVPGrprtegrnqlvLD--LSRPDVVDYIIETLDNLLQEAPIDYV 187
 
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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