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Conserved domains on  [gi|133778924|ref|NP_038491|]
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alpha-galactosidase A precursor [Mus musculus]

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 ...
41-324 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: 575.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924   41 TPTMGWLHWERFMCNLDCQEEPDACISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQRFPSGIK 120
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  121 HLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQTFADWGVDLLKFDGCHcDSVVSLENGYKYMALALNRTGRSI 200
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  201 VYSCEWPLYL-RPFHKPNYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYQKEIVEVAGPGSWNDPDMLVIGNFGLSW 279
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 133778924  280 DQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQD 324
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
Melibiase_2_C pfam17450
Alpha galactosidase A C-terminal beta sandwich domain;
327-413 2.74e-33

Alpha galactosidase A C-terminal beta sandwich domain;


:

Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 120.15  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  327 GKQGYCFRKENHIEVWERPLSNLAWAVAVRNLQEIGGPCPYTIQISSLGRGLACNPGCIITQLLPEKvHLGFYEWTLTLK 406
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79

                  ....*..
gi 133778924  407 TRVNPSG 413
Cdd:pfam17450  80 VSVNPTG 86
 
Name Accession Description Interval E-value
Melibiase_2 pfam16499
Alpha galactosidase A;
41-324 0e+00

Alpha galactosidase A;


Pssm-ID: 374582 [Multi-domain]  Cd Length: 284  Bit Score: 575.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924   41 TPTMGWLHWERFMCNLDCQEEPDACISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQRFPSGIK 120
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  121 HLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQTFADWGVDLLKFDGCHcDSVVSLENGYKYMALALNRTGRSI 200
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  201 VYSCEWPLYL-RPFHKPNYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYQKEIVEVAGPGSWNDPDMLVIGNFGLSW 279
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 133778924  280 DQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQD 324
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
GH27 cd14792
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
42-324 1.12e-139

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: 400.01  E-value: 1.12e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  42 PTMGWLHWERFMCNldcqeepdacISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQRFPSGIKH 121
Cdd:cd14792    1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 122 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSV-VSLENGYKYMALALNRTGR 198
Cdd:cd14792   71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 199 SIVYSCEWPLYLRPfhkpnYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYQkEIVEVAGPGSWNDPDMLVIGNFGL- 277
Cdd:cd14792  151 PIVLSLSWWGYPDP-----WGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLA-EYAAPAGPGHWNDPDMLEVGNGGLg 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 133778924 278 SWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQD 324
Cdd:cd14792  225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
PLN02808 PLN02808
alpha-galactosidase
34-357 3.37e-94

alpha-galactosidase


Pssm-ID: 166449 [Multi-domain]  Cd Length: 386  Bit Score: 288.40  E-value: 3.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  34 LDNGLARTPTMGWLHWERFMCNldcqeepdacISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQ 113
Cdd:PLN02808  24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 114 RFPSGIKHLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSVVSLENgYKYMALA 192
Cdd:PLN02808  94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSPQER-YPKMSKA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 193 LNRTGRSIVYS-CEWPlylrpfHKPNYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYqkeiVEVAGPGSWNDPDMLV 271
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADQNDRW----ASYARPGGWNDPDMLE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 272 IGNFGLSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFRKENHIEVWERPLSNLAW 351
Cdd:PLN02808 243 VGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLSKKRV 322

                 ....*.
gi 133778924 352 AVAVRN 357
Cdd:PLN02808 323 AVVLWN 328
Melibiase_2_C pfam17450
Alpha galactosidase A C-terminal beta sandwich domain;
327-413 2.74e-33

Alpha galactosidase A C-terminal beta sandwich domain;


Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 120.15  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  327 GKQGYCFRKENHIEVWERPLSNLAWAVAVRNLQEIGGPCPYTIQISSLGRGLACNPGCIITQLLPEKvHLGFYEWTLTLK 406
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79

                  ....*..
gi 133778924  407 TRVNPSG 413
Cdd:pfam17450  80 VSVNPTG 86
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
32-136 1.19e-12

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 66.92  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  32 RALDNGLARTPTMGWLHWERFmcnldcqeEPDacISEQLFMQMAELMvsdgwRDAGYDYLCIDDCWMAPERDSK---GRL 108
Cdd:COG3345   24 RLAPGPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDDTaglGDW 88
                         90       100
                 ....*....|....*....|....*...
gi 133778924 109 QADPQRFPSGIKHLANYVHSKGLKLGIY 136
Cdd:COG3345   89 LVDPEKFPNGLKPLADRIHALGMKFGLW 116
 
Name Accession Description Interval E-value
Melibiase_2 pfam16499
Alpha galactosidase A;
41-324 0e+00

Alpha galactosidase A;


Pssm-ID: 374582 [Multi-domain]  Cd Length: 284  Bit Score: 575.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924   41 TPTMGWLHWERFMCNLDCQEEPDACISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQRFPSGIK 120
Cdd:pfam16499   1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  121 HLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQTFADWGVDLLKFDGCHcDSVVSLENGYKYMALALNRTGRSI 200
Cdd:pfam16499  81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  201 VYSCEWPLYL-RPFHKPNYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYQKEIVEVAGPGSWNDPDMLVIGNFGLSW 279
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 133778924  280 DQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQD 324
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
GH27 cd14792
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
42-324 1.12e-139

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: 400.01  E-value: 1.12e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  42 PTMGWLHWERFMCNldcqeepdacISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQRFPSGIKH 121
Cdd:cd14792    1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 122 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSV-VSLENGYKYMALALNRTGR 198
Cdd:cd14792   71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 199 SIVYSCEWPLYLRPfhkpnYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYQkEIVEVAGPGSWNDPDMLVIGNFGL- 277
Cdd:cd14792  151 PIVLSLSWWGYPDP-----WGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLA-EYAAPAGPGHWNDPDMLEVGNGGLg 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 133778924 278 SWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQD 324
Cdd:cd14792  225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
PLN02808 PLN02808
alpha-galactosidase
34-357 3.37e-94

alpha-galactosidase


Pssm-ID: 166449 [Multi-domain]  Cd Length: 386  Bit Score: 288.40  E-value: 3.37e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  34 LDNGLARTPTMGWLHWERFMCNldcqeepdacISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQ 113
Cdd:PLN02808  24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 114 RFPSGIKHLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSVVSLENgYKYMALA 192
Cdd:PLN02808  94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSPQER-YPKMSKA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 193 LNRTGRSIVYS-CEWPlylrpfHKPNYTDIQYYCNHWRNFDDVYDSWESIKNILSWTVVYqkeiVEVAGPGSWNDPDMLV 271
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADQNDRW----ASYARPGGWNDPDMLE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 272 IGNFGLSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFRKENHIEVWERPLSNLAW 351
Cdd:PLN02808 243 VGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLSKKRV 322

                 ....*.
gi 133778924 352 AVAVRN 357
Cdd:PLN02808 323 AVVLWN 328
PLN02229 PLN02229
alpha-galactosidase
27-357 5.42e-91

alpha-galactosidase


Pssm-ID: 177874 [Multi-domain]  Cd Length: 427  Bit Score: 281.44  E-value: 5.42e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  27 SILGVRALDNGLARTPTMGWLHWERFMCNldcqeepdacISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKG 106
Cdd:PLN02229  48 SMYGRLQLNNGLARTPQMGWNSWNFFACN----------INETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSKG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 107 RLQADPQRFPSGIKHLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSVVSLENgY 186
Cdd:PLN02229 118 QLVPDPKTFPSGIKLLADYVHSKGLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCYNLGIKPIER-Y 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 187 KYMALALNRTGRSIVYS-CEWplylrpfhkpNYTDIQYYC----NHWRNFDDVYDSWESIKNILSwtvvYQKEIVEVAGP 261
Cdd:PLN02229 197 PPMRDALNATGRSIFYSlCEW----------GVDDPALWAgkvgNSWRTTDDINDTWASMTTIAD----LNNKWAAYAGP 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 262 GSWNDPDMLVIGNFGLSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFR---KENH 338
Cdd:PLN02229 263 GGWNDPDMLEVGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQangKNGC 342
                        330
                 ....*....|....*....
gi 133778924 339 IEVWERPLSNLAWAVAVRN 357
Cdd:PLN02229 343 QQVWAGPLSGDRLVVALWN 361
PLN02692 PLN02692
alpha-galactosidase
34-369 4.55e-90

alpha-galactosidase


Pssm-ID: 178295 [Multi-domain]  Cd Length: 412  Bit Score: 278.46  E-value: 4.55e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  34 LDNGLARTPTMGWLHWERFMCNLDcqeepdacisEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAPERDSKGRLQADPQ 113
Cdd:PLN02692  48 LANGLGITPPMGWNSWNHFSCKID----------EKMIKETADALVSTGLSKLGYTYVNIDDCWAEIARDEKGNLVPKKS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 114 RFPSGIKHLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSVVSLENgYKYMALA 192
Cdd:PLN02692 118 TFPSGIKALADYVHSKGLKLGIYSDAGYFTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCNNDGSKPTVR-YPVMTRA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 193 LNRTGRSIVYS-CEW-----PLYLRPFHkpnytdiqyycNHWRNFDDVYDSWESIKNILSWTVVYqkeiVEVAGPGSWND 266
Cdd:PLN02692 197 LMKAGRPIFFSlCEWgdmhpALWGSKVG-----------NSWRTTNDISDTWDSMISRADMNEVY----AELARPGGWND 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 267 PDMLVIGNFGLSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFRKENHIEVWERPL 346
Cdd:PLN02692 262 PDMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDVRNMTKETMDIVANKEVIAVNQDPLGVQAKKVRMEGDLEIWAGPL 341
                        330       340
                 ....*....|....*....|...
gi 133778924 347 SNLAWAVAVRNLqeigGPCPYTI 369
Cdd:PLN02692 342 SGYRVALLLLNR----GPWRNSI 360
GH_D cd14790
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
42-319 6.89e-47

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: 161.64  E-value: 6.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  42 PTMGWLHWERFMcnldcqeepdACISEQLFMQMAELMVSDGWrdaGYDYLCIDDCWMApeRDSKGRLQADPQRFPSGiKH 121
Cdd:cd14790    1 PPMGWLTWERYR----------QDIDEMLFMEMADRIAEDEL---PYKVFNIDDCWAK--KDAEGDFVPDPERFPRG-EA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 122 LANYVHSKGLKLGIYADvgnktcagfPGSFGSYDIDAQTFADWGVDLLKFDGCHCDSVVSLEN-----------GYKYMA 190
Cdd:cd14790   65 MARRLHARGLKLGIWGD---------PFRLDWVEDDLQTLAEWGVDMFKLDFGESSGTPVQWFpqkmpnkeqaqGYEQMA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 191 LALNRTGRSIVYSCEWPLYLRPFHKpnytdiqyyCNHWRNFDDVYDSWESIKNILSWTVVYQkeIVEVAGPGSWNDPDML 270
Cdd:cd14790  136 RALNATGEPIVYSGSWSAYQGGGEI---------CNLWRNYDDIQDSWDAVLSIVDWFFTNQ--DVLQAGGFHFNDPDML 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 133778924 271 VIGNFGLSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVI 319
Cdd:cd14790  205 IIGNFGLSAEQSRSQMALWTIMDAPLLMSTDLSTISPSDKKILVNRLMI 253
Melibiase_2_C pfam17450
Alpha galactosidase A C-terminal beta sandwich domain;
327-413 2.74e-33

Alpha galactosidase A C-terminal beta sandwich domain;


Pssm-ID: 407508 [Multi-domain]  Cd Length: 86  Bit Score: 120.15  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  327 GKQGYCFRKENHIEVWERPLSNLAWAVAVRNLQEIGGPCPYTIQISSLGRGLACNPGCIITQLLPEKvHLGFYEWTLTLK 406
Cdd:pfam17450   1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79

                  ....*..
gi 133778924  407 TRVNPSG 413
Cdd:pfam17450  80 VSVNPTG 86
PLN02899 PLN02899
alpha-galactosidase
9-322 9.79e-24

alpha-galactosidase


Pssm-ID: 178487 [Multi-domain]  Cd Length: 633  Bit Score: 103.72  E-value: 9.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924   9 DTRLVCELALCPLALVFWSilGVRAlDNGLARTPTMGWLHWERFmcnldcqeepdaC--ISEQLFMQMAELmVSDGWRDA 86
Cdd:PLN02899   1 KRAQIFFILFCLLSLSLWI--GASS-QQQLASFPPRGWNSYDSF------------SwiVSEEEFLQNAEI-VSQRLLPF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  87 GYDYLCIDDCWMAPER-------------DSKGRLQADPQRFPS-----GIKHLANYVHSKGLKLGIY------------ 136
Cdd:PLN02899  65 GYEYVVVDYLWYRKKVegayvdslgfdviDEWGRPIPDPGRWPSsrggkGFTEVAEKVHAMGLKFGIHvmrgistqavna 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 137 ----------------------ADVG--NKTCAGFPGSFGSYDIDA-----------QTFADWGVDLLKFDgCHCDSVVS 181
Cdd:PLN02899 145 ntpildavkggayeesgrqwraKDIAlkERACAWMSHGFMSVNTKLgagkaflrslyDQYAEWGVDFVKHD-CVFGDDFD 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 182 LENgYKYMALALNRTGRSIVYScewplyLRPFHKPNYT---DIQYYCNHWRNFDDVYDSWESIKniLSWTVVYQKEIVEV 258
Cdd:PLN02899 224 LEE-ITYVSEVLKELDRPIVYS------LSPGTSATPTmakEVSGLVNMYRITGDDWDTWGDVA--AHFDVSRDFAAAGL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 259 AG-PG----SWNDPDMLVIG-------NFG------LSWDQQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIA 320
Cdd:PLN02899 295 IGaKGlrgrSWPDLDMLPLGwltdpgsNVGphracnLTLDEQKTQMTLWAMAKSPLMYGGDLRKLDQATYSLITNPTLLE 374

                 ..
gi 133778924 321 IN 322
Cdd:PLN02899 375 IN 376
PLN03231 PLN03231
putative alpha-galactosidase; Provisional
66-327 1.46e-20

putative alpha-galactosidase; Provisional


Pssm-ID: 178770 [Multi-domain]  Cd Length: 357  Bit Score: 92.35  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  66 ISEQLFMQMAELmVSDGWRDAGYDYLCIDDCWMAPER----------------DSKGRLQADPQRFPS-----GIKHLAN 124
Cdd:PLN03231  15 ISEEQFLENAKI-VSETLKPHGYEYVVIDYLWYRKLKhgwfktsakspgydliDKWGRPLPDPKRWPSttggkGFAPIAA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 125 YVHSKGLKLGIY-------ADVGNKT------------------------CAGFPGSFGSYDIDAQ-----------TFA 162
Cdd:PLN03231  94 KVHALGLKLGIHvmrgistTAVKKKTpilgafksnghawnakdialmdqaCPWMQQCFVGVNTSSEggklfiqslydQYA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 163 DWGVDLLKFDgC-------HCDSVVSLENgykymalALNRTGRSIVYScewplyLRPFHKPN---YTDIQYYCNHWRNFD 232
Cdd:PLN03231 174 SWGIDFIKHD-CvfgaenpQLDEILTVSK-------AIRNSGRPMIYS------LSPGDGATpglAARVAQLVNMYRVTG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924 233 DVYDSWESIKNILSWTVVYQKE----IVEVAGPGSWNDPDMLVIG-------------NFGLSWDQQVTQMALWAIMAAP 295
Cdd:PLN03231 240 DDWDDWKYLVKHFDVARDFAAAgliaIPSVVGGKSWVDLDMLPFGrltdpaaaygpyrNSRLSLEEKKTQMTLWAVAKSP 319
                        330       340       350
                 ....*....|....*....|....*....|..
gi 133778924 296 LLMSNDLRQISSQAKALLQNKDVIAINQDPLG 327
Cdd:PLN03231 320 LMFGGDLRRLDNETLSLLTNPTVLEVNSHSTG 351
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
32-136 1.19e-12

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 66.92  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  32 RALDNGLARTPTMGWLHWERFmcnldcqeEPDacISEQLFMQMAELMvsdgwRDAGYDYLCIDDCWMAPERDSK---GRL 108
Cdd:COG3345   24 RLAPGPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDDTaglGDW 88
                         90       100
                 ....*....|....*....|....*...
gi 133778924 109 QADPQRFPSGIKHLANYVHSKGLKLGIY 136
Cdd:COG3345   89 LVDPEKFPNGLKPLADRIHALGMKFGLW 116
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
45-135 2.32e-10

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: 61.09  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  45 GWLHWERFMCNldcqeepdacISEQLFMQMAELMvsdgwRDAGYDYLCIDDCWMAPERDSKGRL---QADPQRFPSGIKH 121
Cdd:cd14791    5 GWNSWYAYYFD----------ITEEKLLELADAA-----AELGVELFVIDDGWFGARNDDYAGLgdwLVDPEKFPDGLKA 69
                         90
                 ....*....|....
gi 133778924 122 LANYVHSKGLKLGI 135
Cdd:cd14791   70 LADRIHALGMKFGL 83
Melibiase pfam02065
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
84-136 8.50e-06

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: 47.39  E-value: 8.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 133778924   84 RDAGYDYLCIDDCWMAPERDSKGRL---QADPQRFPSGIKHLANYVHSKGLKLGIY 136
Cdd:pfam02065  68 ADLGIELFVLDDGWFGHRNDDNSSLgdwFVNPRKFPNGLDPLAKQVHALGMQFGLW 123
Melibiase_C pfam17801
Alpha galactosidase C-terminal beta sandwich domain; This domain is found at the C-terminus of ...
339-419 6.50e-03

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: 35.31  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778924  339 IEVWERPLSNLAWAVAVRNLqeiGGPCPYTIQISSLgrGLACNPGCIITQLlpekvhlgfyeWT------LTLKTRVNPS 412
Cdd:pfam17801   4 LQVWAKPLSNGDVAVALFNR---GGPSTVTVDLSDL--GLPGASSYSVRDL-----------WTgkdlgtGSTSATVPPH 67

                  ....*..
gi 133778924  413 GTVLFRL 419
Cdd:pfam17801  68 GVALLRL 74
 
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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