|
Name |
Accession |
Description |
Interval |
E-value |
| Melibiase_2 |
pfam16499 |
Alpha galactosidase A; |
8-291 |
0e+00 |
|
Alpha galactosidase A;
Pssm-ID: 374582 [Multi-domain] Cd Length: 284 Bit Score: 604.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 8 TPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIR 87
Cdd:pfam16499 1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 88 QLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYcDSLENLADGYKHMSLALNRTGRSI 167
Cdd:pfam16499 81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 168 VYSCEWPLYM-WPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSW 246
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3HG4_A 247 NQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 291
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
|
|
| GH27 |
cd14792 |
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ... |
9-291 |
3.14e-141 |
|
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: 402.70 E-value: 3.14e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 9 PTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQ 88
Cdd:cd14792 1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 89 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSL-ENLADGYKHMSLALNRTGR 165
Cdd:cd14792 71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 166 SIVYSCEWPLYMwpfqkPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVdVAGPGGWNDPDMLVIGNFGL- 244
Cdd:cd14792 151 PIVLSLSWWGYP-----DPWGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEYAA-PAGPGHWNDPDMLEVGNGGLg 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
3HG4_A 245 SWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 291
Cdd:cd14792 225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
|
|
| PLN02808 |
PLN02808 |
alpha-galactosidase |
1-325 |
2.46e-97 |
|
alpha-galactosidase
Pssm-ID: 166449 [Multi-domain] Cd Length: 386 Bit Score: 295.33 E-value: 2.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 1 LDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQ 80
Cdd:PLN02808 24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 81 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENlADGYKHMSLA 159
Cdd:PLN02808 94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSP-QERYPKMSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 160 LNRTGRSIVYS-CEWPlymwpfQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGPGGWNDP 234
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADqndrWASY--------ARPGGWNDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 235 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 314
Cdd:PLN02808 239 DMLEVGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLS 318
|
330
....*....|.
3HG4_A 315 GLAWAVAMINR 325
Cdd:PLN02808 319 KKRVAVVLWNR 329
|
|
| Melibiase_2_C |
pfam17450 |
Alpha galactosidase A C-terminal beta sandwich domain; |
294-380 |
4.07e-42 |
|
Alpha galactosidase A C-terminal beta sandwich domain;
Pssm-ID: 407508 [Multi-domain] Cd Length: 86 Bit Score: 142.87 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 294 GKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKrKLGFYEWTSRLR 373
Cdd:pfam17450 1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79
|
....*..
3HG4_A 374 SHINPTG 380
Cdd:pfam17450 80 VSVNPTG 86
|
|
| GalA |
COG3345 |
Alpha-galactosidase [Carbohydrate transport and metabolism]; |
3-103 |
7.93e-13 |
|
Alpha-galactosidase [Carbohydrate transport and metabolism];
Pssm-ID: 442574 [Multi-domain] Cd Length: 219 Bit Score: 67.31 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 3 NGLARTPTMGWLHWERFmcnldcqeEPDscISEKLFMEMAELMvsegwKDAGYEYLCIDDCWMAPQRD---SEGRLQADP 79
Cdd:COG3345 28 GPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDdtaGLGDWLVDP 92
|
90 100
....*....|....*....|....
3HG4_A 80 QRFPHGIRQLANYVHSKGLKLGIY 103
Cdd:COG3345 93 EKFPNGLKPLADRIHALGMKFGLW 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Melibiase_2 |
pfam16499 |
Alpha galactosidase A; |
8-291 |
0e+00 |
|
Alpha galactosidase A;
Pssm-ID: 374582 [Multi-domain] Cd Length: 284 Bit Score: 604.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 8 TPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIR 87
Cdd:pfam16499 1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 88 QLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYcDSLENLADGYKHMSLALNRTGRSI 167
Cdd:pfam16499 81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 168 VYSCEWPLYM-WPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSW 246
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3HG4_A 247 NQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 291
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
|
|
| GH27 |
cd14792 |
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ... |
9-291 |
3.14e-141 |
|
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: 402.70 E-value: 3.14e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 9 PTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQ 88
Cdd:cd14792 1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 89 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSL-ENLADGYKHMSLALNRTGR 165
Cdd:cd14792 71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 166 SIVYSCEWPLYMwpfqkPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVdVAGPGGWNDPDMLVIGNFGL- 244
Cdd:cd14792 151 PIVLSLSWWGYP-----DPWGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEYAA-PAGPGHWNDPDMLEVGNGGLg 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
3HG4_A 245 SWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 291
Cdd:cd14792 225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
|
|
| PLN02808 |
PLN02808 |
alpha-galactosidase |
1-325 |
2.46e-97 |
|
alpha-galactosidase
Pssm-ID: 166449 [Multi-domain] Cd Length: 386 Bit Score: 295.33 E-value: 2.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 1 LDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQ 80
Cdd:PLN02808 24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 81 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENlADGYKHMSLA 159
Cdd:PLN02808 94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSP-QERYPKMSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 160 LNRTGRSIVYS-CEWPlymwpfQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGPGGWNDP 234
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADqndrWASY--------ARPGGWNDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 235 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 314
Cdd:PLN02808 239 DMLEVGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLS 318
|
330
....*....|.
3HG4_A 315 GLAWAVAMINR 325
Cdd:PLN02808 319 KKRVAVVLWNR 329
|
|
| PLN02229 |
PLN02229 |
alpha-galactosidase |
1-325 |
1.89e-95 |
|
alpha-galactosidase
Pssm-ID: 177874 [Multi-domain] Cd Length: 427 Bit Score: 292.23 E-value: 1.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 1 LDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQ 80
Cdd:PLN02229 55 LNNGLARTPQMGWNSWNFFACN----------INETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSKGQLVPDPK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 81 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYcdsleNLA----DGYKHM 156
Cdd:PLN02229 125 TFPSGIKLLADYVHSKGLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCY-----NLGikpiERYPPM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 157 SLALNRTGRSIVYS-CEWPL---YMWPfqkpnyteiRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGP 228
Cdd:PLN02229 200 RDALNATGRSIFYSlCEWGVddpALWA---------GKVGNSWRTTDDINDTWASMTTIADlnnkWAAY--------AGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 229 GGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLR-QGDN-- 305
Cdd:PLN02229 263 GGWNDPDMLEVGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQaNGKNgc 342
|
330 340
....*....|....*....|
3HG4_A 306 FEVWERPLSGLAWAVAMINR 325
Cdd:PLN02229 343 QQVWAGPLSGDRLVVALWNR 362
|
|
| PLN02692 |
PLN02692 |
alpha-galactosidase |
1-337 |
2.74e-92 |
|
alpha-galactosidase
Pssm-ID: 178295 [Multi-domain] Cd Length: 412 Bit Score: 283.47 E-value: 2.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 1 LDNGLARTPTMGWLHWERFMCNLDcqeepdscisEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQ 80
Cdd:PLN02692 48 LANGLGITPPMGWNSWNHFSCKID----------EKMIKETADALVSTGLSKLGYTYVNIDDCWAEIARDEKGNLVPKKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 81 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENlADGYKHMSLA 159
Cdd:PLN02692 118 TFPSGIKALADYVHSKGLKLGIYSDAGYFTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCNNDGSKP-TVRYPVMTRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 160 LNRTGRSIVYS-CEW----PLyMWPfqkpnyteiRQYCNHWRNFADIDDSWKSIKSILDWtsfnQERIVDVAGPGGWNDP 234
Cdd:PLN02692 197 LMKAGRPIFFSlCEWgdmhPA-LWG---------SKVGNSWRTTNDISDTWDSMISRADM----NEVYAELARPGGWNDP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 235 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 314
Cdd:PLN02692 263 DMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDVRNMTKETMDIVANKEVIAVNQDPLGVQAKKVRMEGDLEIWAGPLS 342
|
330 340
....*....|....*....|...
3HG4_A 315 GLAWAVAMINRqeigGPRSYTIA 337
Cdd:PLN02692 343 GYRVALLLLNR----GPWRNSIT 361
|
|
| GH_D |
cd14790 |
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ... |
9-286 |
7.65e-49 |
|
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: 165.87 E-value: 7.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 9 PTMGWLHWERFMcnldcqeepdSCISEKLFMEMAELMVSEGWkdaGYEYLCIDDCWMApqRDSEGRLQADPQRFPHGiRQ 88
Cdd:cd14790 1 PPMGWLTWERYR----------QDIDEMLFMEMADRIAEDEL---PYKVFNIDDCWAK--KDAEGDFVPDPERFPRG-EA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 89 LANYVHSKGLKLGIYADvgnktcagfPGSFGYYDIDAQTFADWGVDLLKFDGCYC-----------DSLENLADGYKHMS 157
Cdd:cd14790 65 MARRLHARGLKLGIWGD---------PFRLDWVEDDLQTLAEWGVDMFKLDFGESsgtpvqwfpqkMPNKEQAQGYEQMA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 158 LALNRTGRSIVYSCEWPLYMWPFQKpnyteirqyCNHWRNFADIDDSWKSIKSILDWTSFNQerIVDVAGPGGWNDPDML 237
Cdd:cd14790 136 RALNATGEPIVYSGSWSAYQGGGEI---------CNLWRNYDDIQDSWDAVLSIVDWFFTNQ--DVLQAGGFHFNDPDML 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3HG4_A 238 VIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVI 286
Cdd:cd14790 205 IIGNFGLSAEQSRSQMALWTIMDAPLLMSTDLSTISPSDKKILVNRLMI 253
|
|
| Melibiase_2_C |
pfam17450 |
Alpha galactosidase A C-terminal beta sandwich domain; |
294-380 |
4.07e-42 |
|
Alpha galactosidase A C-terminal beta sandwich domain;
Pssm-ID: 407508 [Multi-domain] Cd Length: 86 Bit Score: 142.87 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 294 GKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKrKLGFYEWTSRLR 373
Cdd:pfam17450 1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79
|
....*..
3HG4_A 374 SHINPTG 380
Cdd:pfam17450 80 VSVNPTG 86
|
|
| PLN03231 |
PLN03231 |
putative alpha-galactosidase; Provisional |
33-299 |
5.03e-24 |
|
putative alpha-galactosidase; Provisional
Pssm-ID: 178770 [Multi-domain] Cd Length: 357 Bit Score: 101.98 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 33 ISEKLFMEMAELmVSEGWKDAGYEYLCIDDCWMAPQR----------------DSEGRLQADPQRFP-----HGIRQLAN 91
Cdd:PLN03231 15 ISEEQFLENAKI-VSETLKPHGYEYVVIDYLWYRKLKhgwfktsakspgydliDKWGRPLPDPKRWPsttggKGFAPIAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 92 YVHSKGLKLGIY-------ADVGNKT------------------------CAGFPGSFGYYDIDAQ-----------TFA 129
Cdd:PLN03231 94 KVHALGLKLGIHvmrgistTAVKKKTpilgafksnghawnakdialmdqaCPWMQQCFVGVNTSSEggklfiqslydQYA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 130 DWGVDLLKFDGCYCDSLENLaDGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKpnyTEIRQYCNHWRNFADIDDSWKSIK 209
Cdd:PLN03231 174 SWGIDFIKHDCVFGAENPQL-DEILTVSKAIRNSGRPMIYSLSPGDGATPGLA---ARVAQLVNMYRVTGDDWDDWKYLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 210 SILDWT-SFNQERIVDVAGPGG---WNDPDMLVIG-------------NFGLSWNQQVTQMALWAIMAAPLFMSNDLRHI 272
Cdd:PLN03231 250 KHFDVArDFAAAGLIAIPSVVGgksWVDLDMLPFGrltdpaaaygpyrNSRLSLEEKKTQMTLWAVAKSPLMFGGDLRRL 329
|
330 340
....*....|....*....|....*..
3HG4_A 273 SPQAKALLQDKDVIAINQDPLGKQGYQ 299
Cdd:PLN03231 330 DNETLSLLTNPTVLEVNSHSTGNRNAQ 356
|
|
| PLN02899 |
PLN02899 |
alpha-galactosidase |
4-289 |
2.53e-23 |
|
alpha-galactosidase
Pssm-ID: 178487 [Multi-domain] Cd Length: 633 Bit Score: 102.18 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 4 GLARTPTMGWLHWERFmcnldcqeepdsC--ISEKLFMEMAELmVSEGWKDAGYEYLCIDDCWMAPQR------------ 69
Cdd:PLN02899 26 QLASFPPRGWNSYDSF------------SwiVSEEEFLQNAEI-VSQRLLPFGYEYVVVDYLWYRKKVegayvdslgfdv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 70 -DSEGRLQADPQRFP-----HGIRQLANYVHSKGLKLGIY----------------------------------ADVG-- 107
Cdd:PLN02899 93 iDEWGRPIPDPGRWPssrggKGFTEVAEKVHAMGLKFGIHvmrgistqavnantpildavkggayeesgrqwraKDIAlk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 108 NKTCAGFPGSFGYYDIDA-----------QTFADWGVDLLKFDGCYCDSLEnlADGYKHMSLALNRTGRSIVYSCEWPLY 176
Cdd:PLN02899 173 ERACAWMSHGFMSVNTKLgagkaflrslyDQYAEWGVDFVKHDCVFGDDFD--LEEITYVSEVLKELDRPIVYSLSPGTS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 177 MWPFQKpnyTEIRQYCNHWRNFADIDDSWKSIKSILDWT-SFNQERIVDVAGPGG--WNDPDMLVIG-------NFG--- 243
Cdd:PLN02899 251 ATPTMA---KEVSGLVNMYRITGDDWDTWGDVAAHFDVSrDFAAAGLIGAKGLRGrsWPDLDMLPLGwltdpgsNVGphr 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
3HG4_A 244 ---LSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAIN 289
Cdd:PLN02899 328 acnLTLDEQKTQMTLWAMAKSPLMYGGDLRKLDQATYSLITNPTLLEIN 376
|
|
| GH36 |
cd14791 |
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ... |
12-282 |
6.53e-13 |
|
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: 68.79 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 12 GWLHWERFMCNldcqeepdscISEKLFMEMAELMvsegwKDAGYEYLCIDDCWMAPQRDSEGRL---QADPQRFPHGIRQ 88
Cdd:cd14791 5 GWNSWYAYYFD----------ITEEKLLELADAA-----AELGVELFVIDDGWFGARNDDYAGLgdwLVDPEKFPDGLKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 89 LANYVHSKGLKLGI-----YADVGNKTCAGFP------------GSFGYY--DI---DAQTF---------ADWGVDLLK 137
Cdd:cd14791 70 LADRIHALGMKFGLwlepeMVGPDSELYREHPdwllkdpggppvTGRNQYvlDLsnpEVRDYlrevidrllREWGIDYLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 138 FDGCY------CDSLENLADGYKHMSLAL--------NRTGRSIVYSC--EWPLYMWPfqkpnyteIRQYCNHWRnFADI 201
Cdd:cd14791 150 WDFNRagaeggSRALDSQGEGLHRYVEALyrlldrlrEAFPDVLIEGCssGGGRPDLG--------MLGYVDQFR-ISDN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 202 DDSwKSIKSILDWTSFnqerivdvAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQ 281
Cdd:cd14791 221 TDA-LERLRIQAGRSL--------LYPPEAMDPDVVLLPNHQTGRLEPLETRAAVAMLGGRLGLSDDLTKLSEEELELLK 291
|
.
3HG4_A 282 D 282
Cdd:cd14791 292 E 292
|
|
| GalA |
COG3345 |
Alpha-galactosidase [Carbohydrate transport and metabolism]; |
3-103 |
7.93e-13 |
|
Alpha-galactosidase [Carbohydrate transport and metabolism];
Pssm-ID: 442574 [Multi-domain] Cd Length: 219 Bit Score: 67.31 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HG4_A 3 NGLARTPTMGWLHWERFmcnldcqeEPDscISEKLFMEMAELMvsegwKDAGYEYLCIDDCWMAPQRD---SEGRLQADP 79
Cdd:COG3345 28 GPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDdtaGLGDWLVDP 92
|
90 100
....*....|....*....|....
3HG4_A 80 QRFPHGIRQLANYVHSKGLKLGIY 103
Cdd:COG3345 93 EKFPNGLKPLADRIHALGMKFGLW 116
|
|
| Melibiase |
pfam02065 |
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ... |
51-103 |
1.66e-05 |
|
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: 46.62 E-value: 1.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
3HG4_A 51 KDAGYEYLCIDDCWMAPQRDSEGRL---QADPQRFPHGIRQLANYVHSKGLKLGIY 103
Cdd:pfam02065 68 ADLGIELFVLDDGWFGHRNDDNSSLgdwFVNPRKFPNGLDPLAKQVHALGMQFGLW 123
|
|
| Melibiase_C |
pfam17801 |
Alpha galactosidase C-terminal beta sandwich domain; This domain is found at the C-terminus of ... |
303-342 |
2.29e-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: 36.46 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|
3HG4_A 303 GDNFEVWERPLSGLAWAVAMINRqeiGGPRSYTIAVASLG 342
Cdd:pfam17801 1 DGDLQVWAKPLSNGDVAVALFNR---GGPSTVTVDLSDLG 37
|
|
| |
