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Conserved domains on  [gi|224487857|sp|P86179|]
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RecName: Full=L-rhamnose-binding lectin CSL3

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
101-194 2.07e-52

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: 163.05  E-value: 2.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 101 ISSIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDP 180
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857 181 CVGTYKYLDVAYTC 194
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
1-94 9.25e-52

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: 161.50  E-value: 9.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   1 AISITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDP 80
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857  81 CVGTYKYLDTKYSC 94
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
 
Name Accession Description Interval E-value
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
101-194 2.07e-52

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: 163.05  E-value: 2.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 101 ISSIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDP 180
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857 181 CVGTYKYLDVAYTC 194
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
1-94 9.25e-52

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: 161.50  E-value: 9.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   1 AISITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDP 80
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857  81 CVGTYKYLDTKYSC 94
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
Gal_Lectin pfam02140
Galactose binding lectin domain;
115-194 6.18e-23

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 87.35  E-value: 6.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857  115 CDRGE-IRIQRANYGRRQHDVCsigrpHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFG-DPCVGTYKYLDVAY 192
Cdd:pfam02140   3 CPPGKvISILFASYGRPDGTTC-----PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGgDPCPGTYKYLEVEY 77

                  ..
gi 224487857  193 TC 194
Cdd:pfam02140  78 KC 79
Gal_Lectin pfam02140
Galactose binding lectin domain;
13-94 9.72e-22

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 84.26  E-value: 9.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   13 LQC-DGAKIHIKRANYGRRQHDVCSigrpdNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFG-DPCVGTYKYLDT 90
Cdd:pfam02140   1 LSCpPGKVISILFASYGRPDGTTCP-----SFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGgDPCPGTYKYLEV 75

                  ....
gi 224487857   91 KYSC 94
Cdd:pfam02140  76 EYKC 79
PLN03059 PLN03059
beta-galactosidase; Provisional
109-194 2.49e-05

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 44.22  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 109 SDSQLLCDRGE--IRIQRANYGRRQHDVCSigrphqqLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVF-GDPCVGTY 185
Cdd:PLN03059 758 PKAHLWCPPGQkiSKIKFASFGVPQGTCGS-------FREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFgGDPCPDSM 830

                 ....*....
gi 224487857 186 KYLDVAYTC 194
Cdd:PLN03059 831 KKLSVEAVC 839
 
Name Accession Description Interval E-value
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
101-194 2.07e-52

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: 163.05  E-value: 2.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 101 ISSIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDP 180
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857 181 CVGTYKYLDVAYTC 194
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
1-94 9.25e-52

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: 161.50  E-value: 9.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   1 AISITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDP 80
Cdd:cd22832    1 ASSITCEGSDAQLDCDGGKIRIQRANYGRRDHDVCSIGRPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDP 80
                         90
                 ....*....|....
gi 224487857  81 CVGTYKYLDTKYSC 94
Cdd:cd22832   81 CVGTYKYLDVAYTC 94
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
102-194 7.17e-37

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: 123.55  E-value: 7.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 102 SSIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPC 181
Cdd:cd22836    3 TSVTCEGGYAVLKCGSGVIQIISANYGRTDSTTCSAGRPASQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSDPC 82
                         90
                 ....*....|...
gi 224487857 182 VGTYKYLDVAYTC 194
Cdd:cd22836   83 VGTYKYLYVTYSC 95
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
103-194 3.71e-35

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: 118.94  E-value: 3.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 103 SIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSqsTTSKMAERCDGKRQCIVSVSNSVFGDPC 181
Cdd:cd22835    2 LVACEGSLAHLKCDEGQvISVYGADYGRRDKTTCSFGRPPSQIQNVECSN--PTDKVAERCNGKNSCSIKASNSVFGDPC 79
                         90
                 ....*....|...
gi 224487857 182 VGTYKYLDVAYTC 194
Cdd:cd22835   80 VGTYKYLEVAYTC 92
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
3-94 1.25e-33

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: 115.08  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22836    4 SVTCEGGYAVLKCGSGVIQIISANYGRTDSTTCSAGRPASQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVFSDPCV 83
                         90
                 ....*....|..
gi 224487857  83 GTYKYLDTKYSC 94
Cdd:cd22836   84 GTYKYLYVTYSC 95
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
104-194 1.26e-33

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: 114.99  E-value: 1.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 104 IICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCsigrPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCV 182
Cdd:cd22827    2 RVCEGQTLTISCPAGKvIDIVSANYGRTDSSTC----PSGGIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCV 77
                         90
                 ....*....|..
gi 224487857 183 GTYKYLDVAYTC 194
Cdd:cd22827   78 GTYKYLEVRYRC 89
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
3-94 1.02e-32

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: 112.78  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCD-GAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSqsSTSKMAERCGGKSECIVPASNFVFGDPC 81
Cdd:cd22835    2 LVACEGSLAHLKCDeGQVISVYGADYGRRDKTTCSFGRPPSQIQNVECSN--PTDKVAERCNGKNSCSIKASNSVFGDPC 79
                         90
                 ....*....|...
gi 224487857  82 VGTYKYLDTKYSC 94
Cdd:cd22835   80 VGTYKYLEVAYTC 92
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
4-94 4.72e-31

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: 108.45  E-value: 4.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCD-GAKIHIKRANYGRRQHDVCsigrPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22827    2 RVCEGQTLTISCPaGKVIDIVSANYGRTDSSTC----PSGGIKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPCV 77
                         90
                 ....*....|..
gi 224487857  83 GTYKYLDTKYSC 94
Cdd:cd22827   78 GTYKYLEVRYRC 89
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
103-194 1.95e-29

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: 104.46  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 103 SIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFgDPCV 182
Cdd:cd22834    5 SITCEGSPVSLDCGPDVIKIYDANYGRRDSTTCSHGRPESQLTNTNCYLPETTKVMSERCNGKSLCDLLASNVVT-DPCY 83
                         90
                 ....*....|..
gi 224487857 183 GTYKYLDVAYTC 194
Cdd:cd22834   84 GTYKYLEVSYSC 95
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
3-94 2.19e-28

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: 101.77  E-value: 2.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFgDPCV 82
Cdd:cd22834    5 SITCEGSPVSLDCGPDVIKIYDANYGRRDSTTCSHGRPESQLTNTNCYLPETTKVMSERCNGKSLCDLLASNVVT-DPCY 83
                         90
                 ....*....|..
gi 224487857  83 GTYKYLDTKYSC 94
Cdd:cd22834   84 GTYKYLEVSYSC 95
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
106-194 1.24e-27

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: 99.62  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 106 CEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSigrPHQQLK-NTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCVG 183
Cdd:cd22830    5 CEGSQLTLECEDGTvIRIIRANYGRFSIAICN---DHGNTDwSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPCPG 81
                         90
                 ....*....|.
gi 224487857 184 TYKYLDVAYTC 194
Cdd:cd22830   82 TPKYLEVHYQC 92
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
3-94 3.13e-26

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: 96.15  E-value: 3.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQC-DGAKIHIKRANYGRRQHDVCSigrpDNQLTD--TNCLSQSSTSKMAERCGGKSECIVPASNFVFGD 79
Cdd:cd22830    2 AYACEGSQLTLECeDGTVIRIIRANYGRFSIAICN----DHGNTDwsVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGD 77
                         90
                 ....*....|....*
gi 224487857  80 PCVGTYKYLDTKYSC 94
Cdd:cd22830   78 PCPGTPKYLEVHYQC 92
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
4-95 2.85e-25

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: 93.87  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDA-LLQCDGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22833    4 TTCDGNNVhRLSCDTGVINVQSALYGRTDSETCSEGRPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSDPCP 83
                         90
                 ....*....|...
gi 224487857  83 GTYKYLDTKYSCV 95
Cdd:cd22833   84 GTYKYLQTNYTCL 96
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
103-194 1.10e-24

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: 92.18  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 103 SIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSIGRPHQQlkNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPC 181
Cdd:cd22823    1 ATACEGETLTLSCPSGQvIKILSAFYGRTDGTTCCCGPNNTS--DTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPC 78
                         90
                 ....*....|...
gi 224487857 182 VGTYKYLDVAYTC 194
Cdd:cd22823   79 PGTSKYLEVTYTC 91
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
104-194 1.92e-24

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: 91.94  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 104 IICEGSDSQLL-CDRGEIRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCV 182
Cdd:cd22833    4 TTCDGNNVHRLsCDTGVINVQSALYGRTDSETCSEGRPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSDPCP 83
                         90
                 ....*....|..
gi 224487857 183 GTYKYLDVAYTC 194
Cdd:cd22833   84 GTYKYLQTNYTC 95
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
102-194 2.88e-24

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: 91.22  E-value: 2.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 102 SSIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCsigrPH-QQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGD 179
Cdd:cd22826    2 REIACEGYKIRLRCPGSDvIMIESANYGRTDSSTC----PSdPNMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPD 77
                         90
                 ....*....|....*
gi 224487857 180 PCVGTYKYLDVAYTC 194
Cdd:cd22826   78 PCPGTFKYLEVIYEC 92
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
3-94 5.33e-24

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: 90.45  E-value: 5.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCDGAK-IHIKRANYGRRQHDVCSigrPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPC 81
Cdd:cd22826    3 EIACEGYKIRLRCPGSDvIMIESANYGRTDSSTCP---SDPNMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC 79
                         90
                 ....*....|...
gi 224487857  82 VGTYKYLDTKYSC 94
Cdd:cd22826   80 PGTFKYLEVIYEC 92
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
3-94 5.25e-23

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: 87.94  E-value: 5.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQC-DGAKIHIKRANYGRRQHDVCSigRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPC 81
Cdd:cd22823    1 ATACEGETLTLSCpSGQVIKILSAFYGRTDGTTCC--CGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPC 78
                         90
                 ....*....|...
gi 224487857  82 VGTYKYLDTKYSC 94
Cdd:cd22823   79 PGTSKYLEVTYTC 91
Gal_Lectin pfam02140
Galactose binding lectin domain;
115-194 6.18e-23

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 87.35  E-value: 6.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857  115 CDRGE-IRIQRANYGRRQHDVCsigrpHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFG-DPCVGTYKYLDVAY 192
Cdd:pfam02140   3 CPPGKvISILFASYGRPDGTTC-----PSFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGgDPCPGTYKYLEVEY 77

                  ..
gi 224487857  193 TC 194
Cdd:pfam02140  78 KC 79
Gal_Lectin pfam02140
Galactose binding lectin domain;
13-94 9.72e-22

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 84.26  E-value: 9.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   13 LQC-DGAKIHIKRANYGRRQHDVCSigrpdNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFG-DPCVGTYKYLDT 90
Cdd:pfam02140   1 LSCpPGKVISILFASYGRPDGTTCP-----SFIQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGgDPCPGTYKYLEV 75

                  ....
gi 224487857   91 KYSC 94
Cdd:pfam02140  76 EYKC 79
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
104-194 1.55e-21

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: 84.01  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 104 IICEGSDSQLLCDRGEIRIQRANYGRRQHDVCSIGRPHqqlkNTNCLSqSTTSKMAERCDGKRQCIVSVSNSVFGDPCVG 183
Cdd:cd22837    2 IICENDSATITCSPETINVISAFYGRTDSTTCSHGRPS----TTNCSS-DTLAYIRALCQGKQTCTLQASNSVFGDPCPG 76
                         90
                 ....*....|.
gi 224487857 184 TYKYLDVAYTC 194
Cdd:cd22837   77 TYKYLRITYSC 87
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
100-194 9.89e-21

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: 82.14  E-value: 9.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 100 TISSIICEGSDSQLLCDRGEIRIQRANYGRRQHDVCsigrPHQQ-LKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFG 178
Cdd:cd22841    1 TETFIVCEGDTDVIDCGNGVINIHSAVYGRTDSTTC----SHDQsVSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFG 76
                         90
                 ....*....|....*.
gi 224487857 179 DPCVGTYKYLDVAYTC 194
Cdd:cd22841   77 DPCPGTYKYLNVTYTC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
101-194 6.99e-20

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: 80.00  E-value: 6.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 101 ISSIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSIGRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGD 179
Cdd:cd22829    2 KSKVVCEGEKLRLSCKPSSrLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81
                         90
                 ....*....|....*.
gi 224487857 180 PCV-GTYKYLDVAYTC 194
Cdd:cd22829   82 PCPpGVRKYLKVVYTC 97
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
4-94 2.97e-19

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: 78.24  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSIGRPdnqlTDTNCLSqSSTSKMAERCGGKSECIVPASNFVFGDPCVG 83
Cdd:cd22837    2 IICENDSATITCSPETINVISAFYGRTDSTTCSHGRP----STTNCSS-DTLAYIRALCQGKQTCTLQASNSVFGDPCPG 76
                         90
                 ....*....|.
gi 224487857  84 TYKYLDTKYSC 94
Cdd:cd22837   77 TYKYLRITYSC 87
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
100-194 3.28e-19

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: 78.23  E-value: 3.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 100 TISSIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSigRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVF- 177
Cdd:cd22839    1 PSSVIICEGDVANLSCPEGKyISIRLANYGRFSLGVCN--PSNNIDLSTTCQNDKTLPILQKSCDGKSECSFVVSNKFFf 78
                         90
                 ....*....|....*..
gi 224487857 178 GDPCVGTYKYLDVAYTC 194
Cdd:cd22839   79 EDPCPGTPKYLEATYSC 95
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
2-94 3.42e-18

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: 75.59  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   2 ISITCEGSDALLQCDGAKIHIKRANYGRRQHDVCSigrPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPC 81
Cdd:cd22841    3 TFIVCEGDTDVIDCGNGVINIHSAVYGRTDSTTCS---HDQSVSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPC 79
                         90
                 ....*....|...
gi 224487857  82 VGTYKYLDTKYSC 94
Cdd:cd22841   80 PGTYKYLNVTYTC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
106-194 1.50e-17

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: 74.24  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 106 CEGSDSQLLCDRG-EIRIQRANYGRR--QHDVCSIGRPH---QQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFG- 178
Cdd:cd22828    8 CDGEELTLRCPPNtTISIQSAFYGRSvpSAQLCPSQSGPassTSLEDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFGl 87
                         90
                 ....*....|....*.
gi 224487857 179 DPCVGTYKYLDVAYTC 194
Cdd:cd22828   88 DPCPGTSKYLEVAYKC 103
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
4-94 1.10e-16

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: 71.68  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCDGAK-IHIKRANYGRRQHDVCSigrPDNQLTD-TNCLSQSSTSKMAERCGGKSECIVPASN-FVFGDP 80
Cdd:cd22839    5 IICEGDVANLSCPEGKyISIRLANYGRFSLGVCN---PSNNIDLsTTCQNDKTLPILQKSCDGKSECSFVVSNkFFFEDP 81
                         90
                 ....*....|....
gi 224487857  81 CVGTYKYLDTKYSC 94
Cdd:cd22839   82 CPGTPKYLEATYSC 95
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
4-95 5.04e-15

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: 67.28  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQC-DGAKIHIKRANYGRRQHDVCSIGRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22829    5 VVCEGEKLRLSCkPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGDPCP 84
                         90
                 ....*....|....
gi 224487857  83 -GTYKYLDTKYSCV 95
Cdd:cd22829   85 pGVRKYLKVVYTCV 98
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
3-96 5.88e-15

galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar proteins; Nematogalectin, also called nemgal, is a nematocyst protein with an N-terminal GlyXY domain and a galactose/rhamnose binding lectin domain. There are two nematogalectins, A and B, in Hydra, and they are the products of alternative splicing. They are major components of the nematocyst tubule. Nematogalectin functions as a trimer that could bind to multiple chondroitin glycosaminoglycan molecules and stabilize the chondroitin proteoglycan layer.


Pssm-ID: 438695 [Multi-domain]  Cd Length: 100  Bit Score: 67.30  E-value: 5.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCDG-AKIHIKRANYGRRQHDVCS---IGRPDNQLTDTNclSQSSTSKMAERCGGKSECIVPASNFVFG 78
Cdd:cd22838    4 AIACEGEKLWLQCPQyELIKIKSAFWGRDDKKTCPhppPGLPSNKMCETD--EENVKKKVNDQCQGEQACEVVASNIFFD 81
                         90
                 ....*....|....*....
gi 224487857  79 DP-CVGTYKYLDTKYSCVQ 96
Cdd:cd22838   82 DTiCPDVYKYLKVKYECIP 100
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
4-95 3.58e-14

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: 65.07  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCDGAK-IHIKRANYGRRQHDVCSIGrpDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22844    5 LACEGYPIELRCPGSDvIMVENANYGRTDDKICDAD--PFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCP 82
                         90
                 ....*....|...
gi 224487857  83 GTYKYLDTKYSCV 95
Cdd:cd22844   83 GTYKYLEVQYDCV 95
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
4-95 4.05e-14

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: 65.12  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCDGAK-IHIKRANYGRRQHDVCSigRPDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22846    6 LSCESYPIELRCPGTDvIMIESANYGRTDDKICD--SDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCP 83
                         90
                 ....*....|...
gi 224487857  83 GTYKYLDTKYSCV 95
Cdd:cd22846   84 GTYKYLEVQYECV 96
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
4-95 5.62e-14

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: 64.65  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   4 ITCEGSDALLQCDGAK-IHIKRANYGRRQHDVCSIGrpDNQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCV 82
Cdd:cd22845    5 LSCEGYPIDLRCPGSDvIMIESANYGRTDDKICDAD--PFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDPCP 82
                         90
                 ....*....|...
gi 224487857  83 GTYKYLDTKYSCV 95
Cdd:cd22845   83 GTYKYLEVQYECV 95
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
106-194 5.62e-14

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: 64.65  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 106 CEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSiGRPHQqLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCVGT 184
Cdd:cd22845    7 CEGYPIDLRCPGSDvIMIESANYGRTDDKICD-ADPFQ-MENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDPCPGT 84
                         90
                 ....*....|
gi 224487857 185 YKYLDVAYTC 194
Cdd:cd22845   85 YKYLEVQYEC 94
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
104-194 6.47e-14

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: 64.69  E-value: 6.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 104 IICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSiGRPHQqLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCV 182
Cdd:cd22844    5 LACEGYPIELRCPGSDvIMVENANYGRTDDKICD-ADPFQ-MENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCP 82
                         90
                 ....*....|..
gi 224487857 183 GTYKYLDVAYTC 194
Cdd:cd22844   83 GTYKYLEVQYDC 94
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
106-194 1.36e-13

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: 63.97  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 106 CEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSigRPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVFGDPCVGT 184
Cdd:cd22846    8 CESYPIELRCPGTDvIMIESANYGRTDDKICD--SDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGT 85
                         90
                 ....*....|
gi 224487857 185 YKYLDVAYTC 194
Cdd:cd22846   86 YKYLEVQYEC 95
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
5-94 2.18e-11

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: 58.06  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   5 TCEGSDALLQCD-GAKIHIKRANYGRR--QHDVCSIGRPDNQLT---DTNCLSQSSTSKMAERCGGKSECIVPASNFVFG 78
Cdd:cd22828    7 ACDGEELTLRCPpNTTISIQSAFYGRSvpSAQLCPSQSGPASSTsleDTNCLAPTALQKVVEECQKKRSCRLLVSSRTFG 86
                         90
                 ....*....|....*..
gi 224487857  79 -DPCVGTYKYLDTKYSC 94
Cdd:cd22828   87 lDPCPGTSKYLEVAYKC 103
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
102-194 8.03e-11

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: 56.26  E-value: 8.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 102 SSIICEGSDSQLLCDRGE-IRIQRANYGR-RQHDVCSigrPHQQLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVF-G 178
Cdd:cd22840    3 SSVACEGDPFEISCPSGQrIKVDYASYGAiGTRSTCG---DSVSPAGETCSAPNSLQTMRQRCQGRQSCEIRVLNSLFpN 79
                         90
                 ....*....|....*..
gi 224487857 179 DPCVGTY-KYLDVAYTC 194
Cdd:cd22840   80 DPCPGTSkKYLEYRYRC 96
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
3-94 4.07e-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: 54.34  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCD-GAKIHIKRANYGR-RQHDVCSIGRPDNQltdTNCLSQSSTSKMAERCGGKSECIVPASN-FVFGD 79
Cdd:cd22840    4 SVACEGDPFEISCPsGQRIKVDYASYGAiGTRSTCGDSVSPAG---ETCSAPNSLQTMRQRCQGRQSCEIRVLNsLFPND 80
                         90
                 ....*....|....*.
gi 224487857  80 PCVGTY-KYLDTKYSC 94
Cdd:cd22840   81 PCPGTSkKYLEYRYRC 96
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
103-194 8.87e-10

galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar proteins; Nematogalectin, also called nemgal, is a nematocyst protein with an N-terminal GlyXY domain and a galactose/rhamnose binding lectin domain. There are two nematogalectins, A and B, in Hydra, and they are the products of alternative splicing. They are major components of the nematocyst tubule. Nematogalectin functions as a trimer that could bind to multiple chondroitin glycosaminoglycan molecules and stabilize the chondroitin proteoglycan layer.


Pssm-ID: 438695 [Multi-domain]  Cd Length: 100  Bit Score: 53.43  E-value: 8.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 103 SIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCsIGRPHQQLKNTNCLSQSTTS--KMAERCDGKRQCIVSVSNSVFGD 179
Cdd:cd22838    4 AIACEGEKLWLQCPQYElIKIKSAFWGRDDKKTC-PHPPPGLPSNKMCETDEENVkkKVNDQCQGEQACEVVASNIFFDD 82
                         90
                 ....*....|....*.
gi 224487857 180 P-CVGTYKYLDVAYTC 194
Cdd:cd22838   83 TiCPDVYKYLKVKYEC 98
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
145-194 5.01e-08

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: 48.82  E-value: 5.01e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 224487857 145 KNTNCLSQSTTSKMAERCDGKRQCIVSVSNSV-FGDPCVGTYKYLDVAYTC 194
Cdd:cd22842   41 SKGSCHAPNSLSVVEKACLGKNSCSIPASNSVfFGDPCPGTTKRLAVQATC 91
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
103-194 1.83e-07

galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 (polycystin-1L2) and similar proteins; Polycystin-1L2 is a novel G-protein-coupled receptor that may function as an ion-channel regulator. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminal region of polycystin-1L2. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding domains of Polycystin-1L2 does not form a binding pocket for rhamnose. Therefore, Polycystin-1L2 is unlikely to act as a rhamnose-binding lectin.


Pssm-ID: 438688 [Multi-domain]  Cd Length: 98  Bit Score: 47.35  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 103 SIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVC-----SIGRPHQQlkntNCLSQSTTSKMAERCDGKRQCIVSVSNSV 176
Cdd:cd22831    3 SLACEDYNATLQCGSGQvIEIDDSFYGRNTPHYCrsenpSPPTDSQE----RCSWVDVRDLVAAQCHGLQVCQIPADPSS 78
                         90
                 ....*....|....*...
gi 224487857 177 FGDPCVGTYKYLDVAYTC 194
Cdd:cd22831   79 FGEPCPELGSYLSVEYHC 96
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
3-96 3.48e-07

galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 (polycystin-1L2) and similar proteins; Polycystin-1L2 is a novel G-protein-coupled receptor that may function as an ion-channel regulator. This model corresponds to a galactose/rhamnose-binding lectin domain found at the N-terminal region of polycystin-1L2. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding domains of Polycystin-1L2 does not form a binding pocket for rhamnose. Therefore, Polycystin-1L2 is unlikely to act as a rhamnose-binding lectin.


Pssm-ID: 438688 [Multi-domain]  Cd Length: 98  Bit Score: 46.58  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   3 SITCEGSDALLQCD-GAKIHIKRANYGRRQHDVCSIGRPDNQLTDTN-CLSQSSTSKMAERCGGKSECIVPASNFVFGDP 80
Cdd:cd22831    3 SLACEDYNATLQCGsGQVIEIDDSFYGRNTPHYCRSENPSPPTDSQErCSWVDVRDLVAAQCHGLQVCQIPADPSSFGEP 82
                         90
                 ....*....|....*.
gi 224487857  81 CVGTYKYLDTKYSCVQ 96
Cdd:cd22831   83 CPELGSYLSVEYHCKE 98
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
8-88 1.17e-06

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: 44.97  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857   8 GSDALLQC-DGAKI-HIKRANYGRRQHDVCSigrpdnqLTDTNCLSQSSTSKMAERCGGKSECIVPASNFV-FGDPCVGT 84
Cdd:cd22842    9 GSTLTLSCpAGQVIsSIDFASYGTPTGTCGS-------FSKGSCHAPNSLSVVEKACLGKNSCSIPASNSVfFGDPCPGT 81

                 ....
gi 224487857  85 YKYL 88
Cdd:cd22842   82 TKRL 85
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
102-194 2.15e-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: 44.36  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 102 SSIICEGSDSQLLCDRGE-IRIQRANYGRRQHDVCSigrpHQQLKNTNCLSQSTTSKmaeRCDGKRQCIVSVSNSVFGDP 180
Cdd:cd22843    3 TAFVCFGQEVTIHCPGDGnISIKSATYGYNNSNVCI----YCNSFNCDKDITSPVNK---KCCGKNTCVLTVSDILEGNP 75
                         90
                 ....*....|....
gi 224487857 181 CVGTYKYLDVAYTC 194
Cdd:cd22843   76 CGIGNSYIRVVYTC 89
PLN03059 PLN03059
beta-galactosidase; Provisional
109-194 2.49e-05

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 44.22  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224487857 109 SDSQLLCDRGE--IRIQRANYGRRQHDVCSigrphqqLKNTNCLSQSTTSKMAERCDGKRQCIVSVSNSVF-GDPCVGTY 185
Cdd:PLN03059 758 PKAHLWCPPGQkiSKIKFASFGVPQGTCGS-------FREGSCHAHKSYDAFERNCIGKQSCSVTVAPEVFgGDPCPDSM 830

                 ....*....
gi 224487857 186 KYLDVAYTC 194
Cdd:PLN03059 831 KKLSVEAVC 839
 
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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