|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03059 |
PLN03059 |
beta-galactosidase; Provisional |
6-826 |
0e+00 |
|
beta-galactosidase; Provisional
Pssm-ID: 166698 [Multi-domain] Cd Length: 840 Bit Score: 882.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 6 FTRLLSLFFILITSLSLAKSTiVSHDERAITINGKRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIETYVFWNAHEP 85
Cdd:PLN03059 9 FLLLFLLFLLSSSWVSHGSAS-VSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 86 KRREYDFSGNLDVVRFIKTIQDAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPNMKFRTVNPSFMNEMQNFTTKIVKMMKE 165
Cdd:PLN03059 88 SPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 166 EKLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWLMCQQPNAPQPMLETCNGFYCDQYEPTNP 245
Cdd:PLN03059 168 EKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 246 STPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYHAPLDEFGNL 325
Cdd:PLN03059 248 YKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 326 NQPKWGHLKQLHTVLKSMEKSLTYGNISRIDLGNSIKATIYTTKEGSSCFIGNVNATADALVNFKGKDYHVPAWSVSVLP 405
Cdd:PLN03059 328 REPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFKSKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 406 DCDKEAYNTAKVNTQTSIMtedSSKPERLEWTWRPESAQKMILKGSGDLIAKGLVDQKDVTNDASDYLWYMTRLHLDKKD 485
Cdd:PLN03059 408 DCKTAVFNTARLGAQSSQM---KMNPVGSTFSWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 486 PLWS--RNMTLRVHSNAHVLHAYVNGKYVGNQFVKDGKFDYRFERKVNhLVHGTNHISLLSVSVGLQNYGPFFESGPTGI 563
Cdd:PLN03059 485 GFLKtgQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVK-LTVGINKISLLSVAVGLPNVGLHFETWNAGV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 564 NGPVSLvgyKGEETIEKDLSQHQWDYKIGLNGYNDKLFSIKSVGHQKWANEKLPTGRM-LTWYKAKFKAPLGKEPVIVDL 642
Cdd:PLN03059 564 LGPVTL---KGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQpLTWYKTTFDAPGGNDPLALDM 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 643 NGLGKGEAWINGQSIGRYWPSFNSSddGCKDECDYRGAYGSDKCAFMCGKPTQRWYHVPRSFLNASGhNTITLFEEMGGN 722
Cdd:PLN03059 641 SSMGKGQIWINGQSIGRHWPAYTAH--GSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSG-NLLIVFEEWGGN 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 723 PSMVNFKTVVVGTVCARAHE-------------------HNKVELSC-HNRPISAVKFASFGNPLGHCGSFAVGTCQGDK 782
Cdd:PLN03059 718 PAGISLVKRTTDSVCADIFEgqpalknwqiiasgkvnslQPKAHLWCpPGQKISKIKFASFGVPQGTCGSFREGSCHAHK 797
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 79517234 783 dAAKTVAKECVGKLNCTVNVSSDTFGSTlDCGDSPKKLAVELEC 826
Cdd:PLN03059 798 -SYDAFERNCIGKQSCSVTVAPEVFGGD-PCPDSMKKLSVEAVC 839
|
|
| Glyco_hydro_35 |
pfam01301 |
Glycosyl hydrolases family 35; |
34-338 |
1.42e-165 |
|
Glycosyl hydrolases family 35;
Pssm-ID: 396048 [Multi-domain] Cd Length: 316 Bit Score: 482.14 E-value: 1.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 34 AITINGKRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIETYVFWNAHEPKRREYDFSGNLDVVRFIKTIQDAGLYSV 113
Cdd:pfam01301 1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 114 LRIGPYVCAEWNYGGFPVWLHNMPNMKFRTVNPSFMNEMQNFTTKIVKMMKeeKLFASQGGPIILAQIENEYG--NVISS 191
Cdd:pfam01301 81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 192 YG-AEGKAYIDWCANMANSLDIGVPWLMCQQPN-APQPMLETCNGFYCDQYEPTN--------PSTPKMWTENWTGWFKN 261
Cdd:pfam01301 159 YLrALRKAYKEWGADMALLFTTDGPWGMCLQCGdLPGPDIYATNGFGCGANPPSNfkllrpfsPNKPLMWSEFWTGWFDH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 262 WGGKHPYRTAEDLAFSVARFFQTgGTFQNYYMYHGGTNFGRVAGGPYIT---TSYDYHAPLDEFGNLNqPKWGHLKQLHT 338
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAK-NSSVNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
|
|
| GanA |
COG1874 |
Beta-galactosidase GanA [Carbohydrate transport and metabolism]; |
40-336 |
4.36e-27 |
|
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
Pssm-ID: 441478 [Multi-domain] Cd Length: 609 Bit Score: 117.33 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 40 KRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIET-YVFWNAHEPKRREYDFSGnLDvvRFIKTIQDAGLYSVLRIGP 118
Cdd:COG1874 7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW-LD--RFIDLLHEAGLKVILRTPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 119 YVcaewnyggFPVWL-HNMPNMKFRTVN----------------PSFMNEMQNFTTKIVKMmkeeklfASQGGPIILAQI 181
Cdd:COG1874 84 AA--------PPAWLlKKYPEILPVDADgrrrgfgsrrhycpssPVYREAARRIVRALAER-------YGDHPAVIMWQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 182 ENEYGNVISSYGAEgKAYIDWCANMANSLD--------------------IGVPWLMCQQPNaPQPMLE----------- 230
Cdd:COG1874 149 DNEYGSYDYCDACA-AAFRDWLRERYGTLDalneawgtafwsqrytdwdeIEPPRLTPTTAN-PSLRLDfrrfssdqvle 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 231 ------------------TCN------------------------------------GFYCDQYEPTNPSTPKMWTENWT 256
Cdd:COG1874 227 ylraqrdilreagpdvpvTTNfmgpfpgldywklardldvvswdnypdgsaadpdeiAFAHDLMRGLKGGGPFMVMEQWP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 257 GWFkNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHgGTNFGrvaggpyitTSYDYHAPLDEFGNLNqPKWGHLKQL 336
Cdd:COG1874 307 GWV-NWGPYNPAKRPGQLRLWSLQALAHGADGVNYFQWR-PSRGG---------TEYDHDAPLDHAGRPT-RKFREVREL 374
|
|
| Gal_Rha_Lectin_BGal |
cd22842 |
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ... |
740-826 |
1.63e-26 |
|
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar proteins; The family represents a group of plant beta-galactosidases (BGals), which belong to glycoside hydrolase family 35. They have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. BGals (EC 3.2.1.23), also called Exo-(1->4)-beta-D-galactanase, or lactase, catalyze hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Some family members contain more than one galactose/rhamnose binding lectin domain. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin domains of BGals do not form a binding pocket for rhamnose. Therefore, BGals are unlikely to act as rhamnose-binding lectins.
Pssm-ID: 438699 [Multi-domain] Cd Length: 91 Bit Score: 103.90 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 740 AHEHNKVELSCH-NRPISAVKFASFGNPLGHCGSFAVGTCQGDkDAAKTVAKECVGKLNCTVNVSSDTFGSTlDCGDSPK 818
Cdd:cd22842 6 GGPGSTLTLSCPaGQVISSIDFASYGTPTGTCGSFSKGSCHAP-NSLSVVEKACLGKNSCSIPASNSVFFGD-PCPGTTK 83
|
....*...
gi 79517234 819 KLAVELEC 826
Cdd:cd22842 84 RLAVQATC 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03059 |
PLN03059 |
beta-galactosidase; Provisional |
6-826 |
0e+00 |
|
beta-galactosidase; Provisional
Pssm-ID: 166698 [Multi-domain] Cd Length: 840 Bit Score: 882.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 6 FTRLLSLFFILITSLSLAKSTiVSHDERAITINGKRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIETYVFWNAHEP 85
Cdd:PLN03059 9 FLLLFLLFLLSSSWVSHGSAS-VSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 86 KRREYDFSGNLDVVRFIKTIQDAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPNMKFRTVNPSFMNEMQNFTTKIVKMMKE 165
Cdd:PLN03059 88 SPGNYYFEDRYDLVKFIKVVQAAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 166 EKLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWLMCQQPNAPQPMLETCNGFYCDQYEPTNP 245
Cdd:PLN03059 168 EKLFEPQGGPIILSQIENEYGPVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 246 STPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYHAPLDEFGNL 325
Cdd:PLN03059 248 YKPKMWTEAWTGWYTEFGGAVPNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 326 NQPKWGHLKQLHTVLKSMEKSLTYGNISRIDLGNSIKATIYTTKEGSSCFIGNVNATADALVNFKGKDYHVPAWSVSVLP 405
Cdd:PLN03059 328 REPKWGHLRDLHKAIKLCEPALVSVDPTVTSLGSNQEAHVFKSKSACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 406 DCDKEAYNTAKVNTQTSIMtedSSKPERLEWTWRPESAQKMILKGSGDLIAKGLVDQKDVTNDASDYLWYMTRLHLDKKD 485
Cdd:PLN03059 408 DCKTAVFNTARLGAQSSQM---KMNPVGSTFSWQSYNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDPDE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 486 PLWS--RNMTLRVHSNAHVLHAYVNGKYVGNQFVKDGKFDYRFERKVNhLVHGTNHISLLSVSVGLQNYGPFFESGPTGI 563
Cdd:PLN03059 485 GFLKtgQYPVLTIFSAGHALHVFINGQLAGTVYGELSNPKLTFSQNVK-LTVGINKISLLSVAVGLPNVGLHFETWNAGV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 564 NGPVSLvgyKGEETIEKDLSQHQWDYKIGLNGYNDKLFSIKSVGHQKWANEKLPTGRM-LTWYKAKFKAPLGKEPVIVDL 642
Cdd:PLN03059 564 LGPVTL---KGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQpLTWYKTTFDAPGGNDPLALDM 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 643 NGLGKGEAWINGQSIGRYWPSFNSSddGCKDECDYRGAYGSDKCAFMCGKPTQRWYHVPRSFLNASGhNTITLFEEMGGN 722
Cdd:PLN03059 641 SSMGKGQIWINGQSIGRHWPAYTAH--GSCNGCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSG-NLLIVFEEWGGN 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 723 PSMVNFKTVVVGTVCARAHE-------------------HNKVELSC-HNRPISAVKFASFGNPLGHCGSFAVGTCQGDK 782
Cdd:PLN03059 718 PAGISLVKRTTDSVCADIFEgqpalknwqiiasgkvnslQPKAHLWCpPGQKISKIKFASFGVPQGTCGSFREGSCHAHK 797
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 79517234 783 dAAKTVAKECVGKLNCTVNVSSDTFGSTlDCGDSPKKLAVELEC 826
Cdd:PLN03059 798 -SYDAFERNCIGKQSCSVTVAPEVFGGD-PCPDSMKKLSVEAVC 839
|
|
| Glyco_hydro_35 |
pfam01301 |
Glycosyl hydrolases family 35; |
34-338 |
1.42e-165 |
|
Glycosyl hydrolases family 35;
Pssm-ID: 396048 [Multi-domain] Cd Length: 316 Bit Score: 482.14 E-value: 1.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 34 AITINGKRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIETYVFWNAHEPKRREYDFSGNLDVVRFIKTIQDAGLYSV 113
Cdd:pfam01301 1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 114 LRIGPYVCAEWNYGGFPVWLHNMPNMKFRTVNPSFMNEMQNFTTKIVKMMKeeKLFASQGGPIILAQIENEYG--NVISS 191
Cdd:pfam01301 81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKMK--PLQATNGGPIIMVQVENEYGsyGVDKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 192 YG-AEGKAYIDWCANMANSLDIGVPWLMCQQPN-APQPMLETCNGFYCDQYEPTN--------PSTPKMWTENWTGWFKN 261
Cdd:pfam01301 159 YLrALRKAYKEWGADMALLFTTDGPWGMCLQCGdLPGPDIYATNGFGCGANPPSNfkllrpfsPNKPLMWSEFWTGWFDH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 262 WGGKHPYRTAEDLAFSVARFFQTgGTFQNYYMYHGGTNFGRVAGGPYIT---TSYDYHAPLDEFGNLNqPKWGHLKQLHT 338
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAK-NSSVNLYMFHGGTNFGFTNGANFYGpqtTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
|
|
| GanA |
COG1874 |
Beta-galactosidase GanA [Carbohydrate transport and metabolism]; |
40-336 |
4.36e-27 |
|
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
Pssm-ID: 441478 [Multi-domain] Cd Length: 609 Bit Score: 117.33 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 40 KRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIET-YVFWNAHEPKRREYDFSGnLDvvRFIKTIQDAGLYSVLRIGP 118
Cdd:COG1874 7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW-LD--RFIDLLHEAGLKVILRTPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 119 YVcaewnyggFPVWL-HNMPNMKFRTVN----------------PSFMNEMQNFTTKIVKMmkeeklfASQGGPIILAQI 181
Cdd:COG1874 84 AA--------PPAWLlKKYPEILPVDADgrrrgfgsrrhycpssPVYREAARRIVRALAER-------YGDHPAVIMWQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 182 ENEYGNVISSYGAEgKAYIDWCANMANSLD--------------------IGVPWLMCQQPNaPQPMLE----------- 230
Cdd:COG1874 149 DNEYGSYDYCDACA-AAFRDWLRERYGTLDalneawgtafwsqrytdwdeIEPPRLTPTTAN-PSLRLDfrrfssdqvle 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 231 ------------------TCN------------------------------------GFYCDQYEPTNPSTPKMWTENWT 256
Cdd:COG1874 227 ylraqrdilreagpdvpvTTNfmgpfpgldywklardldvvswdnypdgsaadpdeiAFAHDLMRGLKGGGPFMVMEQWP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 257 GWFkNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHgGTNFGrvaggpyitTSYDYHAPLDEFGNLNqPKWGHLKQL 336
Cdd:COG1874 307 GWV-NWGPYNPAKRPGQLRLWSLQALAHGADGVNYFQWR-PSRGG---------TEYDHDAPLDHAGRPT-RKFREVREL 374
|
|
| Gal_Rha_Lectin_BGal |
cd22842 |
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ... |
740-826 |
1.63e-26 |
|
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar proteins; The family represents a group of plant beta-galactosidases (BGals), which belong to glycoside hydrolase family 35. They have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. BGals (EC 3.2.1.23), also called Exo-(1->4)-beta-D-galactanase, or lactase, catalyze hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Some family members contain more than one galactose/rhamnose binding lectin domain. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin domains of BGals do not form a binding pocket for rhamnose. Therefore, BGals are unlikely to act as rhamnose-binding lectins.
Pssm-ID: 438699 [Multi-domain] Cd Length: 91 Bit Score: 103.90 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 740 AHEHNKVELSCH-NRPISAVKFASFGNPLGHCGSFAVGTCQGDkDAAKTVAKECVGKLNCTVNVSSDTFGSTlDCGDSPK 818
Cdd:cd22842 6 GGPGSTLTLSCPaGQVISSIDFASYGTPTGTCGSFSKGSCHAP-NSLSVVEKACLGKNSCSIPASNSVFFGD-PCPGTTK 83
|
....*...
gi 79517234 819 KLAVELEC 826
Cdd:cd22842 84 RLAVQATC 91
|
|
| GHD |
pfam17834 |
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ... |
347-417 |
3.32e-24 |
|
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like domain found in glycosyl hydrolase family 35 beta galactosidase enzymes.
Pssm-ID: 436079 Cd Length: 72 Bit Score: 96.60 E-value: 3.32e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79517234 347 LTYGNISRIDLGNSIKATIYTTKEG-SSCFIGNVNATADALVNFKGKDYHVPAWSVSVLPDCDKEAYNTAKV 417
Cdd:pfam17834 1 LLSGQYTTTNLGKLQTATVFEKDKGsCVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
|
|
| Gal_Lectin |
pfam02140 |
Galactose binding lectin domain; |
748-826 |
9.14e-19 |
|
Galactose binding lectin domain;
Pssm-ID: 460460 [Multi-domain] Cd Length: 79 Bit Score: 81.18 E-value: 9.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 748 LSC-HNRPISaVKFASFGNPLGH-CGSFAVGT-CQGDkDAAKTVAKECVGKLNCTVNVSSDTFGSTlDCGDSPKKLAVEL 824
Cdd:pfam02140 1 LSCpPGKVIS-ILFASYGRPDGTtCPSFIQGTnCHSP-NSLAIVSKACQGKNSCSVPASNSVFGGD-PCPGTYKYLEVEY 77
|
..
gi 79517234 825 EC 826
Cdd:pfam02140 78 KC 79
|
|
| Gal_Rha_Lectin |
cd22823 |
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ... |
735-826 |
6.41e-07 |
|
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed from a four-stranded antiparallel beta-sheet which packs against an alpha-helix. It was originally described as galactose-binding lectin domain since it was found in a galactose-binding sea urchin egg lectin (SUEL). SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. Galactose/rhamnose-binding lectin domain is also found in many rhamnose-binding lectins, such as Oncorhynchus keta L-rhamnose-binding lectins (CSLs) and Silurus asotus rhamnose-binding lectin (SAL). In addition, the superfamily includes many SUEL/CSLs/SAL homologous proteins, such as plant beta-galactosidases, mammalian latrophilins, Caenorhabditis elegans protein EVA-1 and its homolog, human protein EVA-1 homolog C (also known as C21orf63). Due to the lack of galactose/rhamnose-binding key residues, some superfamily members may not form a binding pocket for galactose/rhamnose. Therefore, they are unlikely to act as galactose/rhamnose-binding lectins.
Pssm-ID: 438682 [Multi-domain] Cd Length: 91 Bit Score: 47.88 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 735 TVCarahEHNKVELSCHNRPISAVKFASFG----NPLGHCGSFAVGTCQGDKDAAKTVAKECVGKLNCTVNVSSDTFGSt 810
Cdd:cd22823 2 TAC----EGETLTLSCPSGQVIKILSAFYGrtdgTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGD- 76
|
90
....*....|....*.
gi 79517234 811 lDCGDSPKKLAVELEC 826
Cdd:cd22823 77 -PCPGTSKYLEVTYTC 91
|
|
| Glyco_hydro_42 |
pfam02449 |
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ... |
50-211 |
2.01e-06 |
|
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.
Pssm-ID: 396834 Cd Length: 376 Bit Score: 50.73 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 50 HYPRSTadmWPDLINKAKDGGLDAIETYVF-WNAHEPKRREYDFSGnLDvvRFIKTIQDAGLYSVLRIGPyvcaewnyGG 128
Cdd:pfam02449 6 QWPEET---WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW-LD--EVIDLLAKAGIKVILATPT--------AA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 129 FPVWL-HNMPNMKFRTVNPSFMNE------------MQNFTTKIVKMMkeEKLFASQGGpIILAQIENEYG-NVISSYGA 194
Cdd:pfam02449 72 PPAWLvKKHPEILPVDADGRRRGFgsrhhycpsspvYREYAARIVEAL--AERYGDHPA-LIGWHIDNEYGcHVSECYCE 148
|
170
....*....|....*...
gi 79517234 195 E-GKAYIDWCANMANSLD 211
Cdd:pfam02449 149 TcERAFRKWLKNRYGTID 166
|
|
| Gal_Rha_Lectin_EVA1_EVA1C_rpt2 |
cd22829 |
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ... |
735-819 |
3.16e-06 |
|
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, human protein EVA-1 homolog C and similar proteins; The family includes Caenorhabditis elegans protein EVA-1 and its homologs, such as human protein EVA-1 homolog C (also known as C21orf63). EVA-1 functions as an UNC-40 coreceptor to enhance attraction to the MADD-4 guidance cue in C. elegans. It also acts as a receptor for slt-1 and is required for the guidance of the AVM pioneer axon to the ventral nerve cord. Human C21orf63 is a type-1 transmembrane heparin-binding protein. Members in this family contain two tandem galactose/rhamnose-binding lectin domains. This model corresponds to the second one. Due to the lack of rhamnose-binding key residues, the second galactose/rhamnose-binding domains of EVA-1 does not form a binding pocket for rhamnose.
Pssm-ID: 438686 [Multi-domain] Cd Length: 99 Bit Score: 46.10 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 735 TVCarahEHNKVELSCHNRPISAVKFASFGNPLG---HCGSFAVG----TCQGDkDAAKTVAKECVGKLNCTVNVSSDTF 807
Cdd:cd22829 5 VVC----EGEKLRLSCKPSSRLAIYSASYGRTLEgsvECPSTPKGdpdeECLSD-VALETVMKRCHGKRRCSLTADSETF 79
|
90
....*....|..
gi 79517234 808 GSTldCGDSPKK 819
Cdd:cd22829 80 GDP--CPPGVRK 89
|
|
| Gal_Rha_Lectin-like_P113 |
cd22843 |
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ... |
735-826 |
8.38e-06 |
|
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to galactose/rhamnose binding lectin-like domain of P113.
Pssm-ID: 438700 [Multi-domain] Cd Length: 89 Bit Score: 44.74 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 735 TVCarahEHNKVELSCHNRPISAVKFASFGNPLGHCGSFAvGTCQGDKDAAKTVAKECVGKLNCTVNVSSDTFGStlDCG 814
Cdd:cd22843 5 FVC----FGQEVTIHCPGDGNISIKSATYGYNNSNVCIYC-NSFNCDKDITSPVNKKCCGKNTCVLTVSDILEGN--PCG 77
|
90
....*....|..
gi 79517234 815 DSPKKLAVELEC 826
Cdd:cd22843 78 IGNSYIRVVYTC 89
|
|
| Gal_Rha_Lectin_LAT2 |
cd22840 |
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ... |
731-826 |
1.94e-05 |
|
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like protein 2 (LAT2) and similar proteins; LAT2 may have a role in pharyngeal pumping during feeding. It contains a galactose/rhamnose binding lectin domain at the N-terminal region. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding domains of LAT2 does not form a binding pocket for rhamnose. Therefore, LAT2 is unlikely to act as a rhamnose-binding lectin.
Pssm-ID: 438697 [Multi-domain] Cd Length: 96 Bit Score: 43.94 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79517234 731 VVVGTVCarahEHNKVELSCHNRPISAVKFASFGNPLGH--CGSFAVG---TCQGDkDAAKTVAKECVGKLNCTVNVSSD 805
Cdd:cd22840 1 ASSSVAC----EGDPFEISCPSGQRIKVDYASYGAIGTRstCGDSVSPageTCSAP-NSLQTMRQRCQGRQSCEIRVLNS 75
|
90 100
....*....|....*....|..
gi 79517234 806 TFGSTLdC-GDSPKKLAVELEC 826
Cdd:cd22840 76 LFPNDP-CpGTSKKYLEYRYRC 96
|
|
| |
