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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  57 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 136
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 1002819364 137 PCLPGVKKYLTVTYACVP 154
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  57 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 136
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 1002819364 137 PCLPGVKKYLTVTYACVP 154
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  57 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 136
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 1002819364 137 PCLPGVKKYLTVTYACVP 154
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  59 KTVCEDQELKLHCHESKFLNIYSATYGRRTqeRDICSSKAerLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPC 138
Cdd:cd22827     1 KRVCEGQTLTISCPAGKVIDIVSANYGRTD--SSTCPSGG--IKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPC 76

                          90
                  ....*....|....
gi 1002819364 139 lPGVKKYLTVTYAC 152
Cdd:cd22827    77 -VGTYKYLEVRYRC 89

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  61 VCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAeRLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPClP 140
Cdd:cd22826     5 ACEGYKIRLRCPGSDVIMIESANYGR--TDSSTCPSDP-NMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC-P 80

                          90
                  ....*....|..
gi 1002819364 141 GVKKYLTVTYAC 152
Cdd:cd22826    81 GTFKYLEVIYEC 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  61 VCEDQELKLHCHESKFLNIYSATYGRRTQerDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPClP 140
Cdd:cd22830     4 ACEGSQLTLECEDGTVIRIIRANYGRFSI--AICNDHGNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPC-P 80

                          90
                  ....*....|..
gi 1002819364 141 GVKKYLTVTYAC 152
Cdd:cd22830    81 GTPKYLEVHYQC 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  57 KNKTVCEDQELKLHChESKFLNIYSATYGRrtQERDICSSK--AERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHF 134
Cdd:cd22836     2 RTSVTCEGGYAVLKC-GSGVIQIISANYGR--TDSTTCSAGrpASQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVF 78

                          90
                  ....*....|....*...
gi 1002819364 135 GSPClPGVKKYLTVTYAC 152
Cdd:cd22836    79 SDPC-VGTYKYLYVTYSC 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  58 NKTVCEDQELKLHCHESKFLNIYSATYGRRTQeRDICSSkAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHF-GS 136
Cdd:cd22840     3 SSVACEGDPFEISCPSGQRIKVDYASYGAIGT-RSTCGD-SVSPAGETCSAPNSLQTMRQRCQGRQSCEIRVLNSLFpND 80

                          90
                  ....*....|....*.
gi 1002819364 137 PCLPGVKKYLTVTYAC 152
Cdd:cd22840    81 PCPGTSKKYLEYRYRC 96

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  62 CEDQELKLHCHESKfLNIYSATYGRRtqERDICSS--KAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPCL 139
Cdd:cd22832     6 CEGSDAQLDCDGGK-IRIQRANYGRR--DHDVCSIgrPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDPCV 82

                          90
                  ....*....|...
gi 1002819364 140 pGVKKYLTVTYAC 152
Cdd:cd22832    83 -GTYKYLDVAYTC 94

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  56 LKNKTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFG 135
Cdd:cd22844     1 MRRELACEGYPIELRCPGSDVIMVENANYGR--TDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP 78

                          90
                  ....*....|....*....
gi 1002819364 136 SPClPGVKKYLTVTYACVP 154
Cdd:cd22844    79 DPC-PGTYKYLEVQYDCVP 96

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  56 LKNKTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFG 135
Cdd:cd22846     2 VRRELSCESYPIELRCPGTDVIMIESANYGR--TDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFP 79

                          90
                  ....*....|....*....
gi 1002819364 136 SPClPGVKKYLTVTYACVP 154
Cdd:cd22846    80 DPC-PGTYKYLEVQYECVP 97

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  60 TVCEDQELKLHChESKFLNIYSATYGRrtQERDICSSKaeRLPPFDCLSYSALQVLSRrCYGKQRCKIIVNNHHFGSPCl 139
Cdd:cd22837     2 IICENDSATITC-SPETINVISAFYGR--TDSTTCSHG--RPSTTNCSSDTLAYIRAL-CQGKQTCTLQASNSVFGDPC- 74

                          90
                  ....*....|...
gi 1002819364 140 PGVKKYLTVTYAC 152
Cdd:cd22837    75 PGTYKYLRITYSC 87

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819364  62 CEDQELKLHCHESkFLNIYSATYGRRtqERDICSSK--AERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNhHFGSPCL 139
Cdd:cd22834     8 CEGSPVSLDCGPD-VIKIYDANYGRR--DSTTCSHGrpESQLTNTNCYLPETTKVMSERCNGKSLCDLLASN-VVTDPCY 83

                          90
                  ....*....|...
gi 1002819364 140 pGVKKYLTVTYAC 152
Cdd:cd22834    84 -GTYKYLEVSYSC 95

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002819364 106 CLSYSALQVLSRRCYGKQRCKIIVNN-HHFGSPClPGVKKYLTVTYAC 152
Cdd:cd22842    45 CHAPNSLSVVEKACLGKNSCSIPASNsVFFGDPC-PGTTKRLAVQATC 91