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Conserved domains on  [gi|257687073|emb|CBC91489|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

beta-galactosidase( domain architecture ID 1000425)

beta-galactosidase catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides

CATH:  3.20.20.80
CAZY:  GH35
EC:  3.2.1.23
Gene Ontology:  GO:0004565|GO:0005975
PubMed:  8535779|7624375|21639842|31731209|20552664

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03059 super family cl31552
beta-galactosidase; Provisional
 37-877 0e+00

beta-galactosidase; Provisional


The actual alignment was detected with superfamily member PLN03059:

Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1017.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  37 NVSYDHRALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIG 116
Cdd:PLN03059  29 SVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 117 SSGLYLHLRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMREAKLFCWQGGPIIMLQIENEYG 196
Cdd:PLN03059 109 AAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYG 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 197 DVEKSYGQKGKDYVKWAASMALGLGAGVPWVMCKQTDAPENIIDACNGYYCDGFKPNSRTKPVLWTEDWDGWYTKWGGSL 276
Cdd:PLN03059 189 PVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGAV 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 277 PHRPAEDLAFAVARFYQRGGSFQNYYMYFGGTNFGRTSGGPFYITSYDYDAPLDEYGLRSEPKWGHLKDLHAAIKLCEPA 356
Cdd:PLN03059 269 PNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPA 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 357 LVAADaPQYRKLGSKQEAHIYHGDgetggKVCAAFLANIDEHKSAHVKFNGQSYTLPPWSVSILPDCRHVAFNTAKVGAQ 436
Cdd:PLN03059 349 LVSVD-PTVTSLGSNQEAHVFKSK-----SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 437 TSVKTVESARPSLgsmsilqkvvrqdnvsyiskSWMA-LKEPIGIWGENNFTFQGLLEHLNVTKDRSDYLWHKTRISVSE 515
Cdd:PLN03059 423 SSQMKMNPVGSTF--------------------SWQSyNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 516 DDisFWKKNGPNSTVSIDSMRDVLRVFVNKQLAGSIVGHW----VKAVQPVRFIQGNNDLLLLTQTVGLQNYGAFLEKDG 591
Cdd:PLN03059 483 DE--GFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELsnpkLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWN 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 592 AGFRGKAKLTGFKNGDLDLSKSSWTYQVGLKGEADKIYTVEHNEKAEWSTLETDASPSIFMWYKTYFDPPAGTDPVVLNL 671
Cdd:PLN03059 561 AGVLGPVTLKGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDM 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 672 ESMGRGQAWVNGQHIGRYWNIISQKDGCDrTCDYRGAYNSDKCTTNCGKPTQTRYHVPRSWLKPSSNLLVLFEETGGNPF 751
Cdd:PLN03059 641 SSMGKGQIWINGQSIGRHWPAYTAHGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPA 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 752 KISVKTVTAGILCGQVSESHyPPLRKWStpdyINGTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCH 831
Cdd:PLN03059 720 GISLVKRTTDSVCADIFEGQ-PALKNWQ----IIASGKVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCH 794

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|....*.
gi 257687073 832 ASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSGTLKTLAVMSRCS 877
Cdd:PLN03059 795 AHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 37-877 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1017.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  37 NVSYDHRALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIG 116
Cdd:PLN03059  29 SVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 117 SSGLYLHLRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMREAKLFCWQGGPIIMLQIENEYG 196
Cdd:PLN03059 109 AAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYG 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 197 DVEKSYGQKGKDYVKWAASMALGLGAGVPWVMCKQTDAPENIIDACNGYYCDGFKPNSRTKPVLWTEDWDGWYTKWGGSL 276
Cdd:PLN03059 189 PVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGAV 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 277 PHRPAEDLAFAVARFYQRGGSFQNYYMYFGGTNFGRTSGGPFYITSYDYDAPLDEYGLRSEPKWGHLKDLHAAIKLCEPA 356
Cdd:PLN03059 269 PNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPA 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 357 LVAADaPQYRKLGSKQEAHIYHGDgetggKVCAAFLANIDEHKSAHVKFNGQSYTLPPWSVSILPDCRHVAFNTAKVGAQ 436
Cdd:PLN03059 349 LVSVD-PTVTSLGSNQEAHVFKSK-----SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 437 TSVKTVESARPSLgsmsilqkvvrqdnvsyiskSWMA-LKEPIGIWGENNFTFQGLLEHLNVTKDRSDYLWHKTRISVSE 515
Cdd:PLN03059 423 SSQMKMNPVGSTF--------------------SWQSyNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 516 DDisFWKKNGPNSTVSIDSMRDVLRVFVNKQLAGSIVGHW----VKAVQPVRFIQGNNDLLLLTQTVGLQNYGAFLEKDG 591
Cdd:PLN03059 483 DE--GFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELsnpkLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWN 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 592 AGFRGKAKLTGFKNGDLDLSKSSWTYQVGLKGEADKIYTVEHNEKAEWSTLETDASPSIFMWYKTYFDPPAGTDPVVLNL 671
Cdd:PLN03059 561 AGVLGPVTLKGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDM 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 672 ESMGRGQAWVNGQHIGRYWNIISQKDGCDrTCDYRGAYNSDKCTTNCGKPTQTRYHVPRSWLKPSSNLLVLFEETGGNPF 751
Cdd:PLN03059 641 SSMGKGQIWINGQSIGRHWPAYTAHGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPA 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 752 KISVKTVTAGILCGQVSESHyPPLRKWStpdyINGTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCH 831
Cdd:PLN03059 720 GISLVKRTTDSVCADIFEGQ-PALKNWQ----IIASGKVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCH 794

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|....*.
gi 257687073 832 ASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSGTLKTLAVMSRCS 877
Cdd:PLN03059 795 AHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
44-348 1.67e-164

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 481.37  E-value: 1.67e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073   44 ALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIGSSGLYLH 123
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  124 LRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMreAKLFCWQGGPIIMLQIENEYG--DVEKS 201
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKM--KPLQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  202 YGQ-KGKDYVKWAASMALGLGAGVPWVMCKQ-TDAPENIIDACNGYYCDGF--------KPNSRTKPVLWTEDWDGWYTK 271
Cdd:pfam01301 159 YLRaLRKAYKEWGADMALLFTTDGPWGMCLQcGDLPGPDIYATNGFGCGANppsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  272 WGGSLPHRPAEDLAFAVARFYQRGGSFqNYYMYFGGTNFGRTSGGPFY---ITSYDYDAPLDEYGLRSePKWGHLKDLHA 348
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKNSSV-NLYMFHGGTNFGFTNGANFYgpqTTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 786-876 5.41e-39

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: 139.34  E-value: 5.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 786 GTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSG 865
Cdd:cd22842    1 ATVNEGGPGSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPG 80

                         90
                 ....*....|.
gi 257687073 866 TLKTLAVMSRC 876
Cdd:cd22842   81 TTKRLAVQATC 91
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
50-346 7.68e-20

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 94.61  E-value: 7.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  50 KRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQT-YVFWNGHEPVKGQYNFEGrydLVKFVKLIGSSGLYLHLRIGP 128
Cdd:COG1874    7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 129 YVcaewnfggFPVWL-RDIPGI----------------EFRTDNEPFKKEmqkfVTKIVDLMreAKLFCwQGGPIIMLQI 191
Cdd:COG1874   84 AA--------PPAWLlKKYPEIlpvdadgrrrgfgsrrHYCPSSPVYREA----ARRIVRAL--AERYG-DHPAVIMWQV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 192 ENEYGD--------------VEKSYG------------------------------------------------------ 203
Cdd:COG1874  149 DNEYGSydycdacaaafrdwLRERYGtldalneawgtafwsqrytdwdeiepprltpttanpslrldfrrfssdqvleyl 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 204 -----------------------QKGKDYVKWAASMALglgagVPWVMCKQTDAPENIIDACNGYYCDGFKPnsrTKPVL 260
Cdd:COG1874  229 raqrdilreagpdvpvttnfmgpFPGLDYWKLARDLDV-----VSWDNYPDGSAADPDEIAFAHDLMRGLKG---GGPFM 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 261 WTEDWDGWyTKWGGSLPHRPAEDLAFAVARFYQRGGSFQNYYMYfggtnfgRTSGGpfyITSYDYDAPLDEYGLRSePKW 340
Cdd:COG1874  301 VMEQWPGW-VNWGPYNPAKRPGQLRLWSLQALAHGADGVNYFQW-------RPSRG---GTEYDHDAPLDHAGRPT-RKF 368


                 ....*.
gi 257687073 341 GHLKDL 346
Cdd:COG1874  369 REVREL 374
 
Name Accession Description Interval E-value
PLN03059 PLN03059
beta-galactosidase; Provisional
 37-877 0e+00

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 1017.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  37 NVSYDHRALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIG 116
Cdd:PLN03059  29 SVSYDHRAFIINGQRRILISGSIHYPRSTPEMWPDLIQKAKDGGLDVIQTYVFWNGHEPSPGNYYFEDRYDLVKFIKVVQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 117 SSGLYLHLRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMREAKLFCWQGGPIIMLQIENEYG 196
Cdd:PLN03059 109 AAGLYVHLRIGPYICAEWNFGGFPVWLKYVPGIEFRTDNGPFKAAMQKFTEKIVDMMKSEKLFEPQGGPIILSQIENEYG 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 197 DVEKSYGQKGKDYVKWAASMALGLGAGVPWVMCKQTDAPENIIDACNGYYCDGFKPNSRTKPVLWTEDWDGWYTKWGGSL 276
Cdd:PLN03059 189 PVEWEIGAPGKAYTKWAADMAVKLGTGVPWVMCKQEDAPDPVIDTCNGFYCENFKPNKDYKPKMWTEAWTGWYTEFGGAV 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 277 PHRPAEDLAFAVARFYQRGGSFQNYYMYFGGTNFGRTSGGPFYITSYDYDAPLDEYGLRSEPKWGHLKDLHAAIKLCEPA 356
Cdd:PLN03059 269 PNRPAEDLAFSVARFIQNGGSFINYYMYHGGTNFGRTAGGPFIATSYDYDAPLDEYGLPREPKWGHLRDLHKAIKLCEPA 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 357 LVAADaPQYRKLGSKQEAHIYHGDgetggKVCAAFLANIDEHKSAHVKFNGQSYTLPPWSVSILPDCRHVAFNTAKVGAQ 436
Cdd:PLN03059 349 LVSVD-PTVTSLGSNQEAHVFKSK-----SACAAFLANYDTKYSVKVTFGNGQYDLPPWSVSILPDCKTAVFNTARLGAQ 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 437 TSVKTVESARPSLgsmsilqkvvrqdnvsyiskSWMA-LKEPIGIWGENNFTFQGLLEHLNVTKDRSDYLWHKTRISVSE 515
Cdd:PLN03059 423 SSQMKMNPVGSTF--------------------SWQSyNEETASAYTDDTTTMDGLWEQINVTRDATDYLWYMTEVHIDP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 516 DDisFWKKNGPNSTVSIDSMRDVLRVFVNKQLAGSIVGHW----VKAVQPVRFIQGNNDLLLLTQTVGLQNYGAFLEKDG 591
Cdd:PLN03059 483 DE--GFLKTGQYPVLTIFSAGHALHVFINGQLAGTVYGELsnpkLTFSQNVKLTVGINKISLLSVAVGLPNVGLHFETWN 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 592 AGFRGKAKLTGFKNGDLDLSKSSWTYQVGLKGEADKIYTVEHNEKAEWSTLETDASPSIFMWYKTYFDPPAGTDPVVLNL 671
Cdd:PLN03059 561 AGVLGPVTLKGLNEGTRDLSGWKWSYKIGLKGEALSLHTITGSSSVEWVEGSLLAQKQPLTWYKTTFDAPGGNDPLALDM 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 672 ESMGRGQAWVNGQHIGRYWNIISQKDGCDrTCDYRGAYNSDKCTTNCGKPTQTRYHVPRSWLKPSSNLLVLFEETGGNPF 751
Cdd:PLN03059 641 SSMGKGQIWINGQSIGRHWPAYTAHGSCN-GCNYAGTFDDKKCRTNCGEPSQRWYHVPRSWLKPSGNLLIVFEEWGGNPA 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 752 KISVKTVTAGILCGQVSESHyPPLRKWStpdyINGTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCH 831
Cdd:PLN03059 720 GISLVKRTTDSVCADIFEGQ-PALKNWQ----IIASGKVNSLQPKAHLWCPPGQKISKIKFASFGVPQGTCGSFREGSCH 794

                        810       820       830       840
                 ....*....|....*....|....*....|....*....|....*.
gi 257687073 832 ASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSGTLKTLAVMSRCS 877
Cdd:PLN03059 795 AHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKLSVEAVCS 840
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
44-348 1.67e-164

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 481.37  E-value: 1.67e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073   44 ALIIAGKRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQTYVFWNGHEPVKGQYNFEGRYDLVKFVKLIGSSGLYLH 123
Cdd:pfam01301   1 SFLIDGKRFRLISGSIHYFRIPPEMWPDRLQKAKALGLNAIETYVFWNLHEPEPGQYDFSGILDLVKFIKLAQEAGLYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  124 LRIGPYVCAEWNFGGFPVWLRDIPGIEFRTDNEPFKKEMQKFVTKIVDLMreAKLFCWQGGPIIMLQIENEYG--DVEKS 201
Cdd:pfam01301  81 LRPGPYICAEWDFGGLPAWLLTVPGIRLRTSDPPFLEAVERYLTALLPKM--KPLQATNGGPIIMVQVENEYGsyGVDKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  202 YGQ-KGKDYVKWAASMALGLGAGVPWVMCKQ-TDAPENIIDACNGYYCDGF--------KPNSRTKPVLWTEDWDGWYTK 271
Cdd:pfam01301 159 YLRaLRKAYKEWGADMALLFTTDGPWGMCLQcGDLPGPDIYATNGFGCGANppsnfkllRPFSPNKPLMWSEFWTGWFDH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  272 WGGSLPHRPAEDLAFAVARFYQRGGSFqNYYMYFGGTNFGRTSGGPFY---ITSYDYDAPLDEYGLRSePKWGHLKDLHA 348
Cdd:pfam01301 239 WGGPHAIRPAEDIAFEVARFLAKNSSV-NLYMFHGGTNFGFTNGANFYgpqTTSYDYDAPIDEAGDPT-PKYGHLKDLIT 316
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 786-876 5.41e-39

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: 139.34  E-value: 5.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 786 GTMSINSVAPEVHLHCEDGHVISSIEFASYGTPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSG 865
Cdd:cd22842    1 ATVNEGGPGSTLTLSCPAGQVISSIDFASYGTPTGTCGSFSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPG 80

                         90
                 ....*....|.
gi 257687073 866 TLKTLAVMSRC 876
Cdd:cd22842   81 TTKRLAVQATC 91
Gal_Lectin pfam02140
Galactose binding lectin domain;
799-876 4.42e-30

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 113.54  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  799 LHCEDGHVISsIEFASYGTPRGS-CDGFSIGK-CHASNSLSIVSEACKGRNSCFIEVSNTAFISDPCSGTLKTLAVMSRC 876
Cdd:pfam02140   1 LSCPPGKVIS-ILFASYGRPDGTtCPSFIQGTnCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLEVEYKC 79
GHD pfam17834
Beta-sandwich domain in beta galactosidase; This entry corresponds to a beta sandwich like ...
 368-433 2.48e-22

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: 91.21  E-value: 2.48e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257687073  368 LGSKQEAHIYHGDGetggKVCAAFLANIDEHKSAHVKFNGQSYTLPPWSVSILPDCRHVAFNTAKV 433
Cdd:pfam17834  11 LGKLQTATVFEKDK----GSCVAFLVNIDDKKDANVTFRGSDYFLPAWSISILPDCKTVVFNTAKV 72
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
50-346 7.68e-20

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 94.61  E-value: 7.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073  50 KRRMLVSAGIHYPRATPEMWSDLIAKSKEGGADVVQT-YVFWNGHEPVKGQYNFEGrydLVKFVKLIGSSGLYLHLRIGP 128
Cdd:COG1874    7 KPFLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIgYFAWNLHEPEEGVFDFDW---LDRFIDLLHEAGLKVILRTPT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 129 YVcaewnfggFPVWL-RDIPGI----------------EFRTDNEPFKKEmqkfVTKIVDLMreAKLFCwQGGPIIMLQI 191
Cdd:COG1874   84 AA--------PPAWLlKKYPEIlpvdadgrrrgfgsrrHYCPSSPVYREA----ARRIVRAL--AERYG-DHPAVIMWQV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 192 ENEYGD--------------VEKSYG------------------------------------------------------ 203
Cdd:COG1874  149 DNEYGSydycdacaaafrdwLRERYGtldalneawgtafwsqrytdwdeiepprltpttanpslrldfrrfssdqvleyl 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 204 -----------------------QKGKDYVKWAASMALglgagVPWVMCKQTDAPENIIDACNGYYCDGFKPnsrTKPVL 260
Cdd:COG1874  229 raqrdilreagpdvpvttnfmgpFPGLDYWKLARDLDV-----VSWDNYPDGSAADPDEIAFAHDLMRGLKG---GGPFM 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 261 WTEDWDGWyTKWGGSLPHRPAEDLAFAVARFYQRGGSFQNYYMYfggtnfgRTSGGpfyITSYDYDAPLDEYGLRSePKW 340
Cdd:COG1874  301 VMEQWPGW-VNWGPYNPAKRPGQLRLWSLQALAHGADGVNYFQW-------RPSRG---GTEYDHDAPLDHAGRPT-RKF 368


                 ....*.
gi 257687073 341 GHLKDL 346
Cdd:COG1874  369 REVREL 374
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 798-876 7.67e-19

galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding lectin SUL-I and similar proteins; SUL-I is a galactose/rhamnose-binding lectin with mitogenic, chemotactic, and cytotoxic activity. These activities can be triggered by binding of the lectin to specific carbohydrate chains on target cells. SUL-I may be involved in self-defense against invading microorganisms. SUL-I is composed of three distinctive domains with a folding structure similar to galactose/rhamnose-binding lectin domain found in proteins such as mammalian latrophilins, Oncorhynchus keta L-rhamnose-binding lectins (CSLs), and Silurus asotus rhamnose-binding lectin (SAL). The family also includes Heliocidaris crassispina D-galactoside-specific lectin, also known as sea urchin egg lectin or SUEL, and Echinometra lucunter L-rhamnose-binding lectin ELEL-1, both of which contain only one galactose/rhamnose-binding lectin domain. SUEL binds D-galactoside. It may play an important role in the activation of eggs triggered by fertilization, or in their subsequent differentiation. The dimeric form is essential for hemagglutination activity of SUEL. ELEL-1 is a rhamnose-binding lectin that also binds alpha-D-melibiose, alpha-D-lactose, beta-D-lactose, methyl-alpha-D-galactopyranoside, methyl-beta-D--galactopyranoside and D-galactose, but not D-arabinose, L-fucose, D-glucose, D-mannose, D-maltose, D-sucrose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-mannosamine-D-xylose, or by glycoproteins orosomucoid, thyroglobulin, ovomucoid and porcine stomach mucin. It shows cation-independent hemagglutinating activity against rabbit and human erythrocytes. ELEL-1 agglutinates cells of Gram-positive bacterial species S. aureus but not those of Gram-negative E. coli.


Pssm-ID: 438684 [Multi-domain]  Cd Length: 89  Bit Score: 81.87  E-value: 7.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 798 HLHCEDGHVISsIEFASYG-TPRGSCDGFSI--GKCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLAVMS 874
Cdd:cd22827   10 TISCPAGKVID-IVSANYGrTDSSTCPSGGIknTNCRASNSLSIVRNRCNGKRSCSVKASNSVF-GDPCVGTYKYLEVRY 87


                 ..
gi 257687073 875 RC 876
Cdd:cd22827   88 RC 89
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 798-876 3.16e-16

second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin (RBL) and similar proteins; RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the second one.


Pssm-ID: 438693 [Multi-domain]  Cd Length: 95  Bit Score: 74.63  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 798 HLHCEDGHVisSIEFASYG-TPRGSCdgfSIGK---------CHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTL 867
Cdd:cd22836   13 VLKCGSGVI--QIISANYGrTDSTTC---SAGRpasqvqntnCYASNSLAIVSQSCNGKKSCTVSASNSVF-SDPCVGTY 86


                 ....*....
gi 257687073 868 KTLAVMSRC 876
Cdd:cd22836   87 KYLYVTYSC 95
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 791-876 1.09e-14

second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius L-rhamnose-binding lectin (SML) and similar proteins; SML is a rhamnose-binding lectin that also binds melibiose, raffinose, D-galactose, L-arabinose, D-fucose, maltose and D-glucose with decreasing affinity. It does not bind D-arabinose, L-fucose, lactose, xylose or 2-deoxy-D-galactose. SML shows strong hemagglutinating activity against rabbit erythrocytes. SML contains two tandem galactose/rhamnose-binding lectin domains. This model corresponds to the second one.


Pssm-ID: 438692 [Multi-domain]  Cd Length: 92  Bit Score: 70.41  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 791 NSVApevHLHCEDGHVISsIEFASYG-TPRGSC----DGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSG 865
Cdd:cd22835    7 GSLA---HLKCDEGQVIS-VYGADYGrRDKTTCsfgrPPSQIQNVECSNPTDKVAERCNGKNSCSIKASNSVF-GDPCVG 81

                         90
                 ....*....|.
gi 257687073 866 TLKTLAVMSRC 876
Cdd:cd22835   82 TYKYLEVAYTC 92
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 796-876 1.10e-14

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: 70.22  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 796 EVHLHCEDGHVISsIEFASYG-TPRGSC----DGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTL 870
Cdd:cd22823    8 TLTLSCPSGQVIK-ILSAFYGrTDGTTCccgpNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVF-GDPCPGTSKYL 85


                 ....*.
gi 257687073 871 AVMSRC 876
Cdd:cd22823   86 EVTYTC 91
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 798-876 1.75e-12

galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and similar proteins; Latrophilin Cirl (calcium-independent receptor for latrotoxin) is an adhesion-type G-protein-coupled receptor (aGPCR) that acts as a molecular sensor and signal transducer that detects and converts mechanical stimuli into a metabotropic response. It functions in mechanosensory neurons by modulating ionotropic receptor currents, the initiating step of cellular mechanosensation. The model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of Latrophilin Cirl.


Pssm-ID: 438687 [Multi-domain]  Cd Length: 92  Bit Score: 63.80  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 798 HLHCEDGHVISSIEfASYGtpRgscdgFSIG------------KCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSG 865
Cdd:cd22830   11 TLECEDGTVIRIIR-ANYG--R-----FSIAicndhgntdwsvNCMSPRSLRVVQERCDGKRSCSIPASSSVF-GDPCPG 81

                         90
                 ....*....|.
gi 257687073 866 TLKTLAVMSRC 876
Cdd:cd22830   82 TPKYLEVHYQC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 796-878 2.82e-12

first 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. Both 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 first one.


Pssm-ID: 438685 [Multi-domain]  Cd Length: 105  Bit Score: 63.84  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 796 EVHLHCEDGHVISsIEFASYG------------TPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFISDPC 863
Cdd:cd22828   12 ELTLRCPPNTTIS-IQSAFYGrsvpsaqlcpsqSGPASSTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFGLDPC 90

                         90
                 ....*....|....*
gi 257687073 864 SGTLKTLAVMSRCSP 878
Cdd:cd22828   91 PGTSKYLEVAYKCRP 105
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 796-876 1.89e-11

galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called lectomedins or latrotoxin receptors, belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: latrophilin-1 (LPHN1), Latrophilin-2 (LPHN2), and Latrophilin-3 (LPHN3). The LPHN1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. LPHN2 and LPHN3, although sharing strong sequence homology to LPHN1, do not bind alpha-latrotoxin. While LPHN3 is also brain specific, LPHN2, is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. All members in this family contain a galactose/rhamnose-binding lectin domain at N-terminus.


Pssm-ID: 438683 [Multi-domain]  Cd Length: 92  Bit Score: 61.18  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 796 EVHLHCEDGHVISsIEFASYG-TPRGSCDGFS---IGKCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLA 871
Cdd:cd22826   10 KIRLRCPGSDVIM-IESANYGrTDSSTCPSDPnmtDTNCYLPDALAIVSQRCNNRTRCNVRADSSFF-PDPCPGTFKYLE 87


                 ....*
gi 257687073 872 VMSRC 876
Cdd:cd22826   88 VIYEC 92
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 799-876 2.55e-10

galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for egg jelly 3 protein (REJ3) and similar proteins; REJ3 is a polycystin-1 protein (components of non-selective cation channels) that is cleaved at the GPS (G-protein-coupled receptor proteolytic site) domain and localizes to the acrosomal region of sea urchin sperm. REJ3 is a multidomain protein containing only one galactose/rhamnose-binding lectin domain at its N-terminus.


Pssm-ID: 438698 [Multi-domain]  Cd Length: 92  Bit Score: 57.87  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 799 LHCEDGHVIssIEFASYG----TPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLAVMS 874
Cdd:cd22841   14 IDCGNGVIN--IHSAVYGrtdsTTCSHDQSVSNTNCHSDDSVNILSACCNGQSQCTVTATNSIF-GDPCPGTYKYLNVTY 90


                 ..
gi 257687073 875 RC 876
Cdd:cd22841   91 TC 92
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 797-876 2.74e-10

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: 57.81  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 797 VHLHCEDGH-VIS-------SIEFASYGT--PRGSCDGFSIGK---CHASNSLSIVSEACKGRNSCFIEVSNTAFISDPC 863
Cdd:cd22840    3 SSVACEGDPfEIScpsgqriKVDYASYGAigTRSTCGDSVSPAgetCSAPNSLQTMRQRCQGRQSCEIRVLNSLFPNDPC 82

                         90
                 ....*....|....
gi 257687073 864 SGTLKT-LAVMSRC 876
Cdd:cd22840   83 PGTSKKyLEYRYRC 96
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 796-878 8.31e-10

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: 56.50  E-value: 8.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 796 EVHLHCEDGHVISsIEFASYG-TPRGS--CDGFSIG----KCHASNSLSIVSEACKGRNSCFIEVsNTAFISDPC-SGTL 867
Cdd:cd22829   11 KLRLSCKPSSRLA-IYSASYGrTLEGSveCPSTPKGdpdeECLSDVALETVMKRCHGKRRCSLTA-DSETFGDPCpPGVR 88

                         90
                 ....*....|.
gi 257687073 868 KTLAVMSRCSP 878
Cdd:cd22829   89 KYLKVVYTCVP 99
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 798-876 6.51e-09

first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta L-rhamnose-binding lectin CSL3 and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1-3. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. CSL2 has hemagglutinating activity towards rabbit erythrocytes and human type B erythrocytes. CSL3 has hemagglutinating activity towards rabbit erythrocytes, human type A erythrocytes, human type B erythrocytes, human type O erythrocytes, and sheep erythrocytes. Their hemagglutinating activities are inhibited by smooth-type lipopolysaccharide (LPS) from different bacterial species. Members in this family contain two tandem galactose-binding lectin domains. This model corresponds to the first and second galactose/rhamnose-binding lectin domains found in Oncorhynchus keta CSL3, as well as the second galactose/rhamnose-binding lectin domain found in Oncorhynchus keta CSL2.


Pssm-ID: 438689 [Multi-domain]  Cd Length: 94  Bit Score: 54.03  E-value: 6.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 798 HLHCEDGHVisSIEFASYGtpRGSCDGFSIGK---------CHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLK 868
Cdd:cd22832   12 QLDCDGGKI--RIQRANYG--RRDHDVCSIGRpanqltntnCLSQSTTSKMAERCDGKSQCIVPASNSVF-GDPCVGTYK 86


                 ....*...
gi 257687073 869 TLAVMSRC 876
Cdd:cd22832   87 YLDVAYTC 94
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 796-876 3.67e-08

galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like protein 1 (LAT1) and similar proteins; LAT1 plays a role in the establishment of anterior-posterior polarity in tissues during embryogenesis. It is required for the alignment of the mitotic spindles and division planes. It may have a role in cell death events and play an essential role in normal defection and oocyte fertilization. LAT1 is involved in sperm function. it operates in pharyngeal pumping during feeding. LAT1 contains a galactose/rhamnose binding lectin domain at the N-terminus.


Pssm-ID: 438696 [Multi-domain]  Cd Length: 95  Bit Score: 51.65  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 796 EVHLHCEDGHVISsIEFASYGTprgscdgFSIGKCHASN------------SLSIVSEACKGRNSCFIEVSNTAFISDPC 863
Cdd:cd22839   11 VANLSCPEGKYIS-IRLANYGR-------FSLGVCNPSNnidlsttcqndkTLPILQKSCDGKSECSFVVSNKFFFEDPC 82

                         90
                 ....*....|...
gi 257687073 864 SGTLKTLAVMSRC 876
Cdd:cd22839   83 PGTPKYLEATYSC 95
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
 60-196 8.40e-07

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: 52.27  E-value: 8.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073   60 HYPRATpemWSDLIAKSKEGGADVVQTYVF-WNGHEPVKGQYNFEGrydLVKFVKLIGSSGLYLHLRIGPyvcaewnfGG 138
Cdd:pfam02449   6 QWPEET---WEEDIRLMKEAGVNVVRIGIFaWAKLEPEEGKYDFEW---LDEVIDLLAKAGIKVILATPT--------AA 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257687073  139 FPVWL-RDIPGIeFRTDNE-------------PFKKEMQKFVTKIVDLMreAKLFcwQGGP-IIMLQIENEYG 196
Cdd:pfam02449  72 PPAWLvKKHPEI-LPVDADgrrrgfgsrhhycPSSPVYREYAARIVEAL--AERY--GDHPaLIGWHIDNEYG 139
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
 789-876 1.97e-06

second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. Its hemagglutinating activity is inhibited by smooth-type lipopolysaccharide (LPS) from Klebsiella pneumoniae, Escherichia coli K-235, Shigella flexneri 1A, Aeromonas salmonicida and Salmonella minnesota and rough-type LPS from S. flexneri, but not by rough-type LPS from E. coli K12 and E. coli EH100. CSL1 agglutinates E. coli K12 and Bacillus subtilis. CSL1 contains two tandem galactose-binding lectin domains. This model corresponds to the second one.


Pssm-ID: 438691 [Multi-domain]  Cd Length: 95  Bit Score: 46.68  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 789 SINSVAPEVHLHCEDGhVISsIEFASYGTPRGS-CDG------FSIGKCHASNSLSIVSEACKGRNSCfiEVSNTAFISD 861
Cdd:cd22834    5 SITCEGSPVSLDCGPD-VIK-IYDANYGRRDSTtCSHgrpesqLTNTNCYLPETTKVMSERCNGKSLC--DLLASNVVTD 80

                         90
                 ....*....|....*
gi 257687073 862 PCSGTLKTLAVMSRC 876
Cdd:cd22834   81 PCYGTYKYLEVSYSC 95
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 795-863 3.50e-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: 45.90  E-value: 3.50e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257687073 795 PEVHLHCEDGHVISsIEFASYGTPRGSCDGFSIGKCHASNSLSIVSEACKGRNSCFIEVsNTAFISDPC 863
Cdd:cd22843   10 QEVTIHCPGDGNIS-IKSATYGYNNSNVCIYCNSFNCDKDITSPVNKKCCGKNTCVLTV-SDILEGNPC 76
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 803-876 8.87e-06

third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin (RBL) and similar proteins; RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the third one.


Pssm-ID: 438694 [Multi-domain]  Cd Length: 87  Bit Score: 44.72  E-value: 8.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257687073 803 DGHVISSIEfASYG-TPRGSCDGFSIGK--CHASNsLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLAVMSRC 876
Cdd:cd22837   14 SPETINVIS-AFYGrTDSTTCSHGRPSTtnCSSDT-LAYIRALCQGKQTCTLQASNSVF-GDPCPGTYKYLRITYSC 87
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 797-878 1.32e-05

galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; Latrophilin-1 (LPHN1), also called adhesion G protein-coupled receptor L1 (ADGRL1), or calcium-independent alpha-latrotoxin receptor 1 (CIRL-1), or lectomedin-2, is a brain-specific calcium-independent receptor that mediates the effect of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN1.


Pssm-ID: 438701 [Multi-domain]  Cd Length: 97  Bit Score: 44.66  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 797 VHLHCEDGHVISsIEFASYG-TPRGSCDG--FSIG--KCHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLA 871
Cdd:cd22844   12 IELRCPGSDVIM-VENANYGrTDDKICDAdpFQMEnvQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPCPGTYKYLE 89


                 ....*..
gi 257687073 872 VMSRCSP 878
Cdd:cd22844   90 VQYDCVP 96
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
 797-878 1.75e-05

galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; Latrophilin-3 (LPHN3), also called adhesion G protein-coupled receptor L3 (ADGRL3), or calcium-independent alpha-latrotoxin receptor 3 (CIRL-3), or lectomedin-3, is a brain-specific calcium-independent receptor that plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. It is involved in the development of glutamatergic synapses in the cortex. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN3.


Pssm-ID: 438703 [Multi-domain]  Cd Length: 99  Bit Score: 44.32  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 797 VHLHCEDGHVISsIEFASYG-TPRGSCDG----FSIGKCHASNSLSIVSEACKGRNSCFIeVSNTAFISDPCSGTLKTLA 871
Cdd:cd22846   13 IELRCPGTDVIM-IESANYGrTDDKICDSdpaqMENIRCYLPDAYKIMSQRCNNRTQCAV-VAGPDVFPDPCPGTYKYLE 90


                 ....*..
gi 257687073 872 VMSRCSP 878
Cdd:cd22846   91 VQYECVP 97
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 797-878 2.29e-05

galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; Latrophilin-2 (LPHN2), also called adhesion G protein-coupled receptor L2 (ADGRL2), or calcium-independent alpha-latrotoxin receptor 2 (CIRL-2), or latrophilin homolog 1 (LPHH1), or lectomedin-1, is ubiquitously distributed calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. It is probably implicated in the regulation of exocytosis. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminus of LPHN2.


Pssm-ID: 438702 [Multi-domain]  Cd Length: 97  Bit Score: 43.85  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 797 VHLHCEDGHVISsIEFASYG-TPRGSCDG--FSIGK--CHASNSLSIVSEACKGRNSCFIEVSNTAFiSDPCSGTLKTLA 871
Cdd:cd22845   12 IDLRCPGSDVIM-IESANYGrTDDKICDAdpFQMENtdCYLPDAYKIMTQRCNNRTQCIVVTGSDVF-PDPCPGTYKYLE 89


                 ....*..
gi 257687073 872 VMSRCSP 878
Cdd:cd22845   90 VQYECVP 96
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
 797-870 1.06e-04

first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus asotus RBL, Scomberomorus niphonius SML and similar proteins; The family includes a group of L-rhamnose-binding lectins, such as Oncorhynchus keta CSL1 and CSL2. CSL1 has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. CSL2 has hemagglutinating activity towards rabbit erythrocytes and human type B erythrocytes. Their hemagglutinating activities are inhibited by smooth-type lipopolysaccharide (LPS) from different bacterial species. The family also includes Silurus asotus rhamnose-binding lectin (RBL) and Scomberomorus niphonius L-rhamnose-binding lectin (SML). RBL, also known as Silurus asotus (catfish) roe lectin (SAL), is a lectin that binds L-rhamnose. It also binds monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose. RBL does not require a Ca2+ ion or free thiol group for its agglutination activity. SML is a rhamnose-binding lectin that also binds melibiose, raffinose, D-galactose, L-arabinose, D-fucose, maltose, and D-glucose with decreasing affinity. It does not bind D-arabinose, L-fucose, lactose, xylose or 2-deoxy-D-galactose. SML shows strong hemagglutinating activity against rabbit erythrocytes. CSL1-2 and SML contain two tandem galactose/rhamnose-binding lectin domains. RBL contains three galactose/rhamnose-binding lectin domains. This model corresponds to the first one.


Pssm-ID: 438690 [Multi-domain]  Cd Length: 97  Bit Score: 41.87  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257687073 797 VH-LHCEDGhVISsIEFASYG-TPRGSCdgfSIGK---------CHASNSLSIVSEACKGRNSCfiEVSNTAFI-SDPCS 864
Cdd:cd22833   11 VHrLSCDTG-VIN-VQSALYGrTDSETC---SEGRppeqltntqCSQSGTLDLLKNRCDGKKVC--ELNTNDFRtSDPCP 83


                 ....*.
gi 257687073 865 GTLKTL 870
Cdd:cd22833   84 GTYKYL 89
 
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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