|
Name |
Accession |
Description |
Interval |
E-value |
| Melibiase_2 |
pfam16499 |
Alpha galactosidase A; |
39-322 |
0e+00 |
|
Alpha galactosidase A;
Pssm-ID: 374582 [Multi-domain] Cd Length: 284 Bit Score: 601.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 39 TPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQRFPHGIR 118
Cdd:pfam16499 1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 119 QLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYcDSLEKLADGYKHMSLALNRTGRSI 198
Cdd:pfam16499 81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 199 VYSCEWPLYM-WPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSW 277
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 109131558 278 NQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 322
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
|
|
| GH27 |
cd14792 |
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ... |
40-322 |
1.36e-138 |
|
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: 397.31 E-value: 1.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 40 PTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQRFPHGIRQ 119
Cdd:cd14792 1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 120 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSL-EKLADGYKHMSLALNRTGR 196
Cdd:cd14792 71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 197 SIVYSCEWPLYMwpfqkPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVdVAGPGGWNDPDMLVIGNFGL- 275
Cdd:cd14792 151 PIVLSLSWWGYP-----DPWGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEYAA-PAGPGHWNDPDMLEVGNGGLg 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 109131558 276 SWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 322
Cdd:cd14792 225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
|
|
| PLN02808 |
PLN02808 |
alpha-galactosidase |
32-356 |
3.80e-96 |
|
alpha-galactosidase
Pssm-ID: 166449 [Multi-domain] Cd Length: 386 Bit Score: 293.79 E-value: 3.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 32 LDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQ 111
Cdd:PLN02808 24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 112 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLEKlADGYKHMSLA 190
Cdd:PLN02808 94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSP-QERYPKMSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 191 LNRTGRSIVYS-CEWPlymwpfQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGPGGWNDP 265
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADqndrWASY--------ARPGGWNDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 266 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 345
Cdd:PLN02808 239 DMLEVGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLS 318
|
330
....*....|.
gi 109131558 346 DLAWAVAMINR 356
Cdd:PLN02808 319 KKRVAVVLWNR 329
|
|
| Melibiase_2_C |
pfam17450 |
Alpha galactosidase A C-terminal beta sandwich domain; |
325-411 |
2.94e-42 |
|
Alpha galactosidase A C-terminal beta sandwich domain;
Pssm-ID: 407508 [Multi-domain] Cd Length: 86 Bit Score: 143.64 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 325 GKQGYQLRQGDNFEVWERPLSDLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKrKLGFYEWTSRLR 404
Cdd:pfam17450 1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79
|
....*..
gi 109131558 405 SHINPTG 411
Cdd:pfam17450 80 VSVNPTG 86
|
|
| GalA |
COG3345 |
Alpha-galactosidase [Carbohydrate transport and metabolism]; |
29-134 |
7.02e-13 |
|
Alpha-galactosidase [Carbohydrate transport and metabolism];
Pssm-ID: 442574 [Multi-domain] Cd Length: 219 Bit Score: 67.69 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 29 ARALDNGLARTPTMGWLHWERFmcnldcqeEPDscISEKLFMEMAELMvsdgwKDAGYEYLCIDDCWMAPQRDLE---GR 105
Cdd:COG3345 23 ARLAPGPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDDTaglGD 87
|
90 100
....*....|....*....|....*....
gi 109131558 106 LQADPQRFPHGIRQLANYVHSKGLKLGIY 134
Cdd:COG3345 88 WLVDPEKFPNGLKPLADRIHALGMKFGLW 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Melibiase_2 |
pfam16499 |
Alpha galactosidase A; |
39-322 |
0e+00 |
|
Alpha galactosidase A;
Pssm-ID: 374582 [Multi-domain] Cd Length: 284 Bit Score: 601.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 39 TPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQRFPHGIR 118
Cdd:pfam16499 1 TPPMGWLHWERFRCNIDCDDDPENCISEQLFMQMADRMAEDGWKDAGYEYVCIDDCWMSKERDKQGRLQADPKRFPSGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 119 QLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYcDSLEKLADGYKHMSLALNRTGRSI 198
Cdd:pfam16499 81 KLADYVHSKGLKLGIYADVGTKTCAGYPGSLGYYDIDAKTFADWGVDLLKFDGCY-SNLEDLVEGYPNMSFALNKTGRPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 199 VYSCEWPLYM-WPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSW 277
Cdd:pfam16499 160 VYSCEWPLYMgGLPQQVNYTEIRKYCNHWRNYDDIQDSWDSVKSIVDWFADNQDVFVPAAGPGGWNDPDMLIIGNFGLSY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 109131558 278 NQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 322
Cdd:pfam16499 240 DQQRTQMALWAIMAAPLFMSNDLRSISPEAKAILQNKDVIAINQD 284
|
|
| GH27 |
cd14792 |
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ... |
40-322 |
1.36e-138 |
|
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: 397.31 E-value: 1.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 40 PTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQRFPHGIRQ 119
Cdd:cd14792 1 PPMGWNSWNAFGCN----------INEKLIKATADAMVSSGLRDAGYEYVNIDDGWQAKRRDADGRLVPDPTRFPSGMKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 120 LANYVHSKGLKLGIYADVGNKTCA--GFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSL-EKLADGYKHMSLALNRTGR 196
Cdd:cd14792 71 LADYVHSKGLKFGIYSDAGTPTCAdgGYPGSLGHEDSDAATFASWGVDYLKYDGCGAPSGrLDAQERYTAMSDALNATGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 197 SIVYSCEWPLYMwpfqkPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVdVAGPGGWNDPDMLVIGNFGL- 275
Cdd:cd14792 151 PIVLSLSWWGYP-----DPWGWAAEIANSWRTTGDIWDSWTSVLSIIDQFADLAEYAA-PAGPGHWNDPDMLEVGNGGLg 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 109131558 276 SWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQD 322
Cdd:cd14792 225 TDDEQRTHFSLWAIMASPLILGNDLRNLDDETLALLTNPEVIAVNQD 271
|
|
| PLN02808 |
PLN02808 |
alpha-galactosidase |
32-356 |
3.80e-96 |
|
alpha-galactosidase
Pssm-ID: 166449 [Multi-domain] Cd Length: 386 Bit Score: 293.79 E-value: 3.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 32 LDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQ 111
Cdd:PLN02808 24 LDNGLGLTPQMGWNSWNHFQCN----------INETLIKQTADAMVSSGLAALGYKYINLDDCWAELKRDSQGNLVPKAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 112 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLEKlADGYKHMSLA 190
Cdd:PLN02808 94 TFPSGIKALADYVHSKGLKLGIYSDAGTLTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSP-QERYPKMSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 191 LNRTGRSIVYS-CEWPlymwpfQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGPGGWNDP 265
Cdd:PLN02808 173 LLNSGRPIFFSlCEWG------QEDPATWAGDIGNSWRTTGDIQDNWDSMTSRADqndrWASY--------ARPGGWNDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 266 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 345
Cdd:PLN02808 239 DMLEVGNGGMTTEEYRSHFSIWALAKAPLLIGCDIRSMDNETFELLSNKEVIAVNQDKLGVQGKKVKKDGDLEVWAGPLS 318
|
330
....*....|.
gi 109131558 346 DLAWAVAMINR 356
Cdd:PLN02808 319 KKRVAVVLWNR 329
|
|
| PLN02229 |
PLN02229 |
alpha-galactosidase |
28-356 |
2.90e-93 |
|
alpha-galactosidase
Pssm-ID: 177874 [Multi-domain] Cd Length: 427 Bit Score: 287.60 E-value: 2.90e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 28 GARALDNGLARTPTMGWLHWERFMCNldcqeepdscISEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQ 107
Cdd:PLN02229 51 GRLQLNNGLARTPQMGWNSWNFFACN----------INETVIKETADALVSTGLADLGYIHVNIDDCWSNLKRDSKGQLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 108 ADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLeKLADGYKHM 187
Cdd:PLN02229 121 PDPKTFPSGIKLLADYVHSKGLKLGIYSDAGVFTCQVRPGSLFHEVDDADIFASWGVDYLKYDNCYNLGI-KPIERYPPM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 188 SLALNRTGRSIVYS-CEWPL---YMWPfqkpnyteiRQYCNHWRNFADIDDSWKSIKSILD----WTSFnqerivdvAGP 259
Cdd:PLN02229 200 RDALNATGRSIFYSlCEWGVddpALWA---------GKVGNSWRTTDDINDTWASMTTIADlnnkWAAY--------AGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 260 GGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLR-QGDN-- 336
Cdd:PLN02229 263 GGWNDPDMLEVGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETMEILSNKEVIAVNQDPLGVQGRKIQaNGKNgc 342
|
330 340
....*....|....*....|
gi 109131558 337 FEVWERPLSDLAWAVAMINR 356
Cdd:PLN02229 343 QQVWAGPLSGDRLVVALWNR 362
|
|
| PLN02692 |
PLN02692 |
alpha-galactosidase |
32-368 |
6.23e-91 |
|
alpha-galactosidase
Pssm-ID: 178295 [Multi-domain] Cd Length: 412 Bit Score: 281.16 E-value: 6.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 32 LDNGLARTPTMGWLHWERFMCNLDcqeepdscisEKLFMEMAELMVSDGWKDAGYEYLCIDDCWMAPQRDLEGRLQADPQ 111
Cdd:PLN02692 48 LANGLGITPPMGWNSWNHFSCKID----------EKMIKETADALVSTGLSKLGYTYVNIDDCWAEIARDEKGNLVPKKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 112 RFPHGIRQLANYVHSKGLKLGIYADVGNKTCAG-FPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSlEKLADGYKHMSLA 190
Cdd:PLN02692 118 TFPSGIKALADYVHSKGLKLGIYSDAGYFTCSKtMPGSLGHEEQDAKTFASWGIDYLKYDNCNNDG-SKPTVRYPVMTRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 191 LNRTGRSIVYS-CEW----PLyMWPfqkpnyteiRQYCNHWRNFADIDDSWKSIKSILDWtsfnQERIVDVAGPGGWNDP 265
Cdd:PLN02692 197 LMKAGRPIFFSlCEWgdmhPA-LWG---------SKVGNSWRTTNDISDTWDSMISRADM----NEVYAELARPGGWNDP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 266 DMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLS 345
Cdd:PLN02692 263 DMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDVRNMTKETMDIVANKEVIAVNQDPLGVQAKKVRMEGDLEIWAGPLS 342
|
330 340
....*....|....*....|...
gi 109131558 346 DLAWAVAMINRqeigGPRSYTIA 368
Cdd:PLN02692 343 GYRVALLLLNR----GPWRNSIT 361
|
|
| GH_D |
cd14790 |
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ... |
40-317 |
1.82e-48 |
|
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: 1.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 40 PTMGWLHWERFMcnldcqeepdSCISEKLFMEMAELMVSDGWkdaGYEYLCIDDCWMApqRDLEGRLQADPQRFPHGiRQ 119
Cdd:cd14790 1 PPMGWLTWERYR----------QDIDEMLFMEMADRIAEDEL---PYKVFNIDDCWAK--KDAEGDFVPDPERFPRG-EA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 120 LANYVHSKGLKLGIYADvgnktcagfPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLEK-----------LADGYKHMS 188
Cdd:cd14790 65 MARRLHARGLKLGIWGD---------PFRLDWVEDDLQTLAEWGVDMFKLDFGESSGTPVqwfpqkmpnkeQAQGYEQMA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 189 LALNRTGRSIVYSCEWPLYMWPFQKpnyteirqyCNHWRNFADIDDSWKSIKSILDWTSFNQerIVDVAGPGGWNDPDML 268
Cdd:cd14790 136 RALNATGEPIVYSGSWSAYQGGGEI---------CNLWRNYDDIQDSWDAVLSIVDWFFTNQ--DVLQAGGFHFNDPDML 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 109131558 269 VIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVI 317
Cdd:cd14790 205 IIGNFGLSAEQSRSQMALWTIMDAPLLMSTDLSTISPSDKKILVNRLMI 253
|
|
| Melibiase_2_C |
pfam17450 |
Alpha galactosidase A C-terminal beta sandwich domain; |
325-411 |
2.94e-42 |
|
Alpha galactosidase A C-terminal beta sandwich domain;
Pssm-ID: 407508 [Multi-domain] Cd Length: 86 Bit Score: 143.64 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 325 GKQGYQLRQGDNFEVWERPLSDLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKrKLGFYEWTSRLR 404
Cdd:pfam17450 1 GKQGRRLKKKDNIEVWERPLSDNSLAVAVLNRREIGMPYRYTLSLAKLGYGKVCSPACNVTDIFPGK-KLGVFELTSNLV 79
|
....*..
gi 109131558 405 SHINPTG 411
Cdd:pfam17450 80 VSVNPTG 86
|
|
| PLN03231 |
PLN03231 |
putative alpha-galactosidase; Provisional |
64-330 |
2.50e-23 |
|
putative alpha-galactosidase; Provisional
Pssm-ID: 178770 [Multi-domain] Cd Length: 357 Bit Score: 100.44 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 64 ISEKLFMEMAELmVSDGWKDAGYEYLCIDDCWM-------------APQRDL---EGRLQADPQRFP-----HGIRQLAN 122
Cdd:PLN03231 15 ISEEQFLENAKI-VSETLKPHGYEYVVIDYLWYrklkhgwfktsakSPGYDLidkWGRPLPDPKRWPsttggKGFAPIAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 123 YVHSKGLKLGIY-------ADVGNKT------------------------CAGFPGSFGYYDIDAQ-----------TFA 160
Cdd:PLN03231 94 KVHALGLKLGIHvmrgistTAVKKKTpilgafksnghawnakdialmdqaCPWMQQCFVGVNTSSEggklfiqslydQYA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 161 DWGVDLLKFDgCYCDSLEKLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKpnyTEIRQYCNHWRNFADIDDSWKSIK 240
Cdd:PLN03231 174 SWGIDFIKHD-CVFGAENPQLDEILTVSKAIRNSGRPMIYSLSPGDGATPGLA---ARVAQLVNMYRVTGDDWDDWKYLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 241 SILDWT-SFNQERIVDVAGPGG---WNDPDMLVIG-------------NFGLSWNQQVTQMALWAIMAAPLFMSNDLRHI 303
Cdd:PLN03231 250 KHFDVArDFAAAGLIAIPSVVGgksWVDLDMLPFGrltdpaaaygpyrNSRLSLEEKKTQMTLWAVAKSPLMFGGDLRRL 329
|
330 340
....*....|....*....|....*..
gi 109131558 304 SPQAKALLQDKDVIAINQDPLGKQGYQ 330
Cdd:PLN03231 330 DNETLSLLTNPTVLEVNSHSTGNRNAQ 356
|
|
| PLN02899 |
PLN02899 |
alpha-galactosidase |
35-320 |
8.69e-23 |
|
alpha-galactosidase
Pssm-ID: 178487 [Multi-domain] Cd Length: 633 Bit Score: 101.02 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 35 GLARTPTMGWLHWERFmcnldcqeepdsC--ISEKLFMEMAELmVSDGWKDAGYEYLCIDDCWMAPQR------------ 100
Cdd:PLN02899 26 QLASFPPRGWNSYDSF------------SwiVSEEEFLQNAEI-VSQRLLPFGYEYVVVDYLWYRKKVegayvdslgfdv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 101 -DLEGRLQADPQRFP-----HGIRQLANYVHSKGLKLGIY----------------------------------ADVG-- 138
Cdd:PLN02899 93 iDEWGRPIPDPGRWPssrggKGFTEVAEKVHAMGLKFGIHvmrgistqavnantpildavkggayeesgrqwraKDIAlk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 139 NKTCAGFPGSFGYYDIDA-----------QTFADWGVDLLKFDGCYCDSLEklADGYKHMSLALNRTGRSIVYSCEWPLY 207
Cdd:PLN02899 173 ERACAWMSHGFMSVNTKLgagkaflrslyDQYAEWGVDFVKHDCVFGDDFD--LEEITYVSEVLKELDRPIVYSLSPGTS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 208 MWPFQKpnyTEIRQYCNHWRNFADIDDSWKSIKSILDWT-SFNQERIVDVAGPGG--WNDPDMLVIG-------NFG--- 274
Cdd:PLN02899 251 ATPTMA---KEVSGLVNMYRITGDDWDTWGDVAAHFDVSrDFAAAGLIGAKGLRGrsWPDLDMLPLGwltdpgsNVGphr 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 109131558 275 ---LSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAIN 320
Cdd:PLN02899 328 acnLTLDEQKTQMTLWAMAKSPLMYGGDLRKLDQATYSLITNPTLLEIN 376
|
|
| GalA |
COG3345 |
Alpha-galactosidase [Carbohydrate transport and metabolism]; |
29-134 |
7.02e-13 |
|
Alpha-galactosidase [Carbohydrate transport and metabolism];
Pssm-ID: 442574 [Multi-domain] Cd Length: 219 Bit Score: 67.69 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 29 ARALDNGLARTPTMGWLHWERFmcnldcqeEPDscISEKLFMEMAELMvsdgwKDAGYEYLCIDDCWMAPQRDLE---GR 105
Cdd:COG3345 23 ARLAPGPPDKPRPVGWNSWEAY--------YFD--FTEEKLLALADAA-----AELGVELFVLDDGWFGGRRDDTaglGD 87
|
90 100
....*....|....*....|....*....
gi 109131558 106 LQADPQRFPHGIRQLANYVHSKGLKLGIY 134
Cdd:COG3345 88 WLVDPEKFPNGLKPLADRIHALGMKFGLW 116
|
|
| GH36 |
cd14791 |
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ... |
43-313 |
2.64e-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: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 43 GWLHWERFMCNldcqeepdscISEKLFMEMAELMvsdgwKDAGYEYLCIDDCWMAPQRDLEGRL---QADPQRFPHGIRQ 119
Cdd:cd14791 5 GWNSWYAYYFD----------ITEEKLLELADAA-----AELGVELFVIDDGWFGARNDDYAGLgdwLVDPEKFPDGLKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 120 LANYVHSKGLKLGI-----YADVGNKTCAGFP------------GSFGYY--DI---DAQTF---------ADWGVDLLK 168
Cdd:cd14791 70 LADRIHALGMKFGLwlepeMVGPDSELYREHPdwllkdpggppvTGRNQYvlDLsnpEVRDYlrevidrllREWGIDYLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 169 FDGCY------CDSLEKLADGYKHMSLAL--------NRTGRSIVYSC--EWPLYMWPfqkpnyteIRQYCNHWRnFADI 232
Cdd:cd14791 150 WDFNRagaeggSRALDSQGEGLHRYVEALyrlldrlrEAFPDVLIEGCssGGGRPDLG--------MLGYVDQFR-ISDN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109131558 233 DDSwKSIKSILDWTSFnqerivdvAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQ 312
Cdd:cd14791 221 TDA-LERLRIQAGRSL--------LYPPEAMDPDVVLLPNHQTGRLEPLETRAAVAMLGGRLGLSDDLTKLSEEELELLK 291
|
.
gi 109131558 313 D 313
Cdd:cd14791 292 E 292
|
|
| Melibiase |
pfam02065 |
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ... |
82-134 |
5.11e-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: 45.08 E-value: 5.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 109131558 82 KDAGYEYLCIDDCWMAPQRDLEGRL---QADPQRFPHGIRQLANYVHSKGLKLGIY 134
Cdd:pfam02065 68 ADLGIELFVLDDGWFGHRNDDNSSLgdwFVNPRKFPNGLDPLAKQVHALGMQFGLW 123
|
|
| Melibiase_C |
pfam17801 |
Alpha galactosidase C-terminal beta sandwich domain; This domain is found at the C-terminus of ... |
334-373 |
8.42e-04 |
|
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: 38.00 E-value: 8.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 109131558 334 GDNFEVWERPLSDLAWAVAMINRqeiGGPRSYTIAVASLG 373
Cdd:pfam17801 1 DGDLQVWAKPLSNGDVAVALFNR---GGPSTVTVDLSDLG 37
|
|
| |
