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Conserved domains on  [gi|2462583019|ref|XP_054180703|]
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protein eva-1 homolog C isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAM176 pfam14851
FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.
 300-440 4.47e-63

FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.


:

Pssm-ID: 464347  Cd Length: 145  Bit Score: 200.22  E-value: 4.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 300 DGILVSNSLAAFAYIRAHPERAALLFVSSVCIGLALTLCALVIRESCAKDFRDLQLGREQLVPGSDKVEEDS--EDEEEE 377
Cdd:pfam14851   1 DMELLSNSLAAYAHIRANPERFALYFVSGVCFGLVLTLCLLVIRISCRPDCRRLRPKKKHLKPESESDEEDSeeEEDEEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583019 378 EDPSESDFPGELSGFCRT-SYPIYSSIEAAELAERIERREQIIQEIWMNSGLDT-SLPRNMGQFY 440
Cdd:pfam14851  81 DDSSDSDFPDELSRFDRTlSVNVFTSAEELERAQRLEERERIIREIWRNGQPDIgSGTRTLGRVY 145
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 163-260 4.82e-48

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: 159.73  E-value: 4.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 242
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 2462583019 243 PCLPGVKKYLTVTYACVP 260
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 61-160 5.93e-43

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: 146.66  E-value: 5.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  61 QNHTTYACDGDYLNLQCPRHSTISVQSAFYGQD---YQMCSSQKPA--SQREDSLTCVAATTFQKVLDECQNQRACHLLV 135
Cdd:cd22828     1 RTFQRHACDGEELTLRCPPNTTISIQSAFYGRSvpsAQLCPSQSGPasSTSLEDTNCLAPTALQKVVEECQKKRSCRLLV 80

                          90       100
                  ....*....|....*....|....*
gi 2462583019 136 NSRVFGPDLCPGSSKYLLVSFKCQP 160
Cdd:cd22828    81 SSRTFGLDPCPGTSKYLEVAYKCRP 105
 
Name Accession Description Interval E-value
FAM176 pfam14851
FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.
 300-440 4.47e-63

FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.


Pssm-ID: 464347  Cd Length: 145  Bit Score: 200.22  E-value: 4.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 300 DGILVSNSLAAFAYIRAHPERAALLFVSSVCIGLALTLCALVIRESCAKDFRDLQLGREQLVPGSDKVEEDS--EDEEEE 377
Cdd:pfam14851   1 DMELLSNSLAAYAHIRANPERFALYFVSGVCFGLVLTLCLLVIRISCRPDCRRLRPKKKHLKPESESDEEDSeeEEDEEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583019 378 EDPSESDFPGELSGFCRT-SYPIYSSIEAAELAERIERREQIIQEIWMNSGLDT-SLPRNMGQFY 440
Cdd:pfam14851  81 DDSSDSDFPDELSRFDRTlSVNVFTSAEELERAQRLEERERIIREIWRNGQPDIgSGTRTLGRVY 145
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 163-260 4.82e-48

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: 159.73  E-value: 4.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 242
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 2462583019 243 PCLPGVKKYLTVTYACVP 260
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 61-160 5.93e-43

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: 146.66  E-value: 5.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  61 QNHTTYACDGDYLNLQCPRHSTISVQSAFYGQD---YQMCSSQKPA--SQREDSLTCVAATTFQKVLDECQNQRACHLLV 135
Cdd:cd22828     1 RTFQRHACDGEELTLRCPPNTTISIQSAFYGRSvpsAQLCPSQSGPasSTSLEDTNCLAPTALQKVVEECQKKRSCRLLV 80

                          90       100
                  ....*....|....*....|....*
gi 2462583019 136 NSRVFGPDLCPGSSKYLLVSFKCQP 160
Cdd:cd22828    81 SSRTFGLDPCPGTSKYLEVAYKCRP 105
Gal_Lectin pfam02140
Galactose binding lectin domain;
75-158 3.25e-22

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 90.04  E-value: 3.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  75 LQCPRHSTISVQSAFYG-QDYQMCSSQkpasqrEDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCPGSSKYLL 153
Cdd:pfam02140   1 LSCPPGKVISILFASYGrPDGTTCPSF------IQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLE 74


                  ....*
gi 2462583019 154 VSFKC 158
Cdd:pfam02140  75 VEYKC 79
Gal_Lectin pfam02140
Galactose binding lectin domain;
175-258 7.34e-21

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 86.19  E-value: 7.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 175 LHCHESKFLNIYSATYGRRTQerDICSSKAERLppfDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS-PClPGVKKYLT 253
Cdd:pfam02140   1 LSCPPGKVISILFASYGRPDG--TTCPSFIQGT---NCHSPNSLAIVSKACQGKNSCSVPASNSVFGGdPC-PGTYKYLE 74


                  ....*
gi 2462583019 254 VTYAC 258
Cdd:pfam02140  75 VEYKC 79
PLN03059 PLN03059
beta-galactosidase; Provisional
 74-158 3.60e-05

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 46.15  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  74 NLQCPRHSTIS-VQSAFYGQDYQMCSSQKPASqredsltCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCPGSSKYL 152
Cdd:PLN03059  761 HLWCPPGQKISkIKFASFGVPQGTCGSFREGS-------CHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKL 833


                  ....*.
gi 2462583019 153 LVSFKC 158
Cdd:PLN03059  834 SVEAVC 839
PLN03059 PLN03059
beta-galactosidase; Provisional
 156-258 7.15e-04

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 41.91  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 156 FKCQPKLKN-------KTVCEDQELKLHC-HESKFLNIYSATYGrrtQERDICSSKAERlppfDCLSYSALQVLSRRCYG 227
Cdd:PLN03059  736 FEGQPALKNwqiiasgKVNSLQPKAHLWCpPGQKISKIKFASFG---VPQGTCGSFREG----SCHAHKSYDAFERNCIG 808

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462583019 228 KQRCKIIVNNHHF-GSPClPGVKKYLTVTYAC 258
Cdd:PLN03059  809 KQSCSVTVAPEVFgGDPC-PDSMKKLSVEAVC 839
 
Name Accession Description Interval E-value
FAM176 pfam14851
FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.
 300-440 4.47e-63

FAM176 family; Members of the FAM176 family regulate autophagy and apoptosis.


Pssm-ID: 464347  Cd Length: 145  Bit Score: 200.22  E-value: 4.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 300 DGILVSNSLAAFAYIRAHPERAALLFVSSVCIGLALTLCALVIRESCAKDFRDLQLGREQLVPGSDKVEEDS--EDEEEE 377
Cdd:pfam14851   1 DMELLSNSLAAYAHIRANPERFALYFVSGVCFGLVLTLCLLVIRISCRPDCRRLRPKKKHLKPESESDEEDSeeEEDEEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462583019 378 EDPSESDFPGELSGFCRT-SYPIYSSIEAAELAERIERREQIIQEIWMNSGLDT-SLPRNMGQFY 440
Cdd:pfam14851  81 DDSSDSDFPDELSRFDRTlSVNVFTSAEELERAQRLEERERIIREIWRNGQPDIgSGTRTLGRVY 145
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 163-260 4.82e-48

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: 159.73  E-value: 4.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 242
Cdd:cd22829     2 KSKVVCEGEKLRLSCKPSSRLAIYSASYGRTLEGSVECPSTPKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFGD 81

                          90
                  ....*....|....*...
gi 2462583019 243 PCLPGVKKYLTVTYACVP 260
Cdd:cd22829    82 PCPPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_EVA1_EVA1C_rpt1 cd22828
first galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 61-160 5.93e-43

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: 146.66  E-value: 5.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  61 QNHTTYACDGDYLNLQCPRHSTISVQSAFYGQD---YQMCSSQKPA--SQREDSLTCVAATTFQKVLDECQNQRACHLLV 135
Cdd:cd22828     1 RTFQRHACDGEELTLRCPPNTTISIQSAFYGRSvpsAQLCPSQSGPasSTSLEDTNCLAPTALQKVVEECQKKRSCRLLV 80

                          90       100
                  ....*....|....*....|....*
gi 2462583019 136 NSRVFGPDLCPGSSKYLLVSFKCQP 160
Cdd:cd22828    81 SSRTFGLDPCPGTSKYLEVAYKCRP 105
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 165-258 6.88e-25

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: 97.57  E-value: 6.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 165 KTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPC 244
Cdd:cd22823     1 ATACEGETLTLSCPSGQVIKILSAFYGR--TDGTTCCCGPNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFGDPC 78

                          90
                  ....*....|....
gi 2462583019 245 lPGVKKYLTVTYAC 258
Cdd:cd22823    79 -PGTSKYLEVTYTC 91
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 165-258 4.78e-24

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: 95.35  E-value: 4.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 165 KTVCEDQELKLHCHESKFLNIYSATYGRRTqeRDICSSKAerLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPC 244
Cdd:cd22827     1 KRVCEGQTLTISCPAGKVIDIVSANYGRTD--SSTCPSGG--IKNTNCRASNSLSIVRNRCNGKRSCSVKASNSVFGDPC 76

                          90
                  ....*....|....
gi 2462583019 245 lPGVKKYLTVTYAC 258
Cdd:cd22827    77 -VGTYKYLEVRYRC 89
Gal_Lectin pfam02140
Galactose binding lectin domain;
75-158 3.25e-22

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 90.04  E-value: 3.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  75 LQCPRHSTISVQSAFYG-QDYQMCSSQkpasqrEDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCPGSSKYLL 153
Cdd:pfam02140   1 LSCPPGKVISILFASYGrPDGTTCPSF------IQGTNCHSPNSLAIVSKACQGKNSCSVPASNSVFGGDPCPGTYKYLE 74


                  ....*
gi 2462583019 154 VSFKC 158
Cdd:pfam02140  75 VEYKC 79
Gal_Lectin pfam02140
Galactose binding lectin domain;
175-258 7.34e-21

Galactose binding lectin domain;


Pssm-ID: 460460 [Multi-domain]  Cd Length: 79  Bit Score: 86.19  E-value: 7.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 175 LHCHESKFLNIYSATYGRRTQerDICSSKAERLppfDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS-PClPGVKKYLT 253
Cdd:pfam02140   1 LSCPPGKVISILFASYGRPDG--TTCPSFIQGT---NCHSPNSLAIVSKACQGKNSCSVPASNSVFGGdPC-PGTYKYLE 74


                  ....*
gi 2462583019 254 VTYAC 258
Cdd:pfam02140  75 VEYKC 79
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 65-158 5.76e-19

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: 81.40  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  65 TYACDGDYLNLQCPRHSTISVQSAFYG-QDYQMCSSQkpaSQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGpD 143
Cdd:cd22823     1 ATACEGETLTLSCPSGQVIKILSAFYGrTDGTTCCCG---PNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNSVFG-D 76

                          90
                  ....*....|....*
gi 2462583019 144 LCPGSSKYLLVSFKC 158
Cdd:cd22823    77 PCPGTSKYLEVTYTC 91
Gal_Rha_Lectin_SUL-I-like cd22827
galactose/rhamnose binding lectin domain found in Toxopneustes pileolus rhamnose-binding ...
 67-158 6.52e-19

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


Pssm-ID: 438684 [Multi-domain]  Cd Length: 89  Bit Score: 81.10  E-value: 6.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYG-QDYQMCSSQKPASQRedsltCVAATTFQKVLDECQNQRACHLLVNSRVFGpDLC 145
Cdd:cd22827     3 VCEGQTLTISCPAGKVIDIVSANYGrTDSSTCPSGGIKNTN-----CRASNSLSIVRNRCNGKRSCSVKASNSVFG-DPC 76

                          90
                  ....*....|...
gi 2462583019 146 PGSSKYLLVSFKC 158
Cdd:cd22827    77 VGTYKYLEVRYRC 89
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
 62-160 1.28e-18

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: 80.78  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  62 NHTTYACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCssQKPASQREDSLTC--VAATTFQKVLDECQNQRACHLLVNSR 138
Cdd:cd22838     1 PNTAIACEGEKLWLQCPQYELIKIKSAFWGRdDKKTC--PHPPPGLPSNKMCetDEENVKKKVNDQCQGEQACEVVASNI 78

                          90       100
                  ....*....|....*....|..
gi 2462583019 139 VFGPDLCPGSSKYLLVSFKCQP 160
Cdd:cd22838    79 FFDDTICPDVYKYLKVKYECIP 100
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 167-258 5.83e-17

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: 75.81  E-value: 5.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 167 VCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAeRLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPClP 246
Cdd:cd22826     5 ACEGYKIRLRCPGSDVIMIESANYGR--TDSSTCPSDP-NMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFFPDPC-P 80

                          90
                  ....*....|..
gi 2462583019 247 GVKKYLTVTYAC 258
Cdd:cd22826    81 GTFKYLEVIYEC 92
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 64-158 9.57e-17

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: 74.97  E-value: 9.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  64 TTYACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSSQkpaSQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGp 142
Cdd:cd22830     1 TAYACEGSQLTLECEDGTVIRIIRANYGRfSIAICNDH---GNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFG- 76

                          90
                  ....*....|....*.
gi 2462583019 143 DLCPGSSKYLLVSFKC 158
Cdd:cd22830    77 DPCPGTPKYLEVHYQC 92
Gal_Rha_Lectin_LPHNs cd22826
galactose/rhamnose binding lectin domain found in latrophilins; Latrophilins, also called ...
 63-158 1.54e-16

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: 74.66  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  63 HTTYACDGDYLNLQCPRHSTISVQSAFYG-QDYQMCssqkPASQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFg 141
Cdd:cd22826     1 KREIACEGYKIRLRCPGSDVIMIESANYGrTDSSTC----PSDPNMTDTNCYLPDALAIVSQRCNNRTRCNVRADSSFF- 75

                          90
                  ....*....|....*..
gi 2462583019 142 PDLCPGSSKYLLVSFKC 158
Cdd:cd22826    76 PDPCPGTFKYLEVIYEC 92
Gal_Rha_Lectin_EVA1_EVA1C_rpt2 cd22829
second galactose/rhamnose binding lectin domain found in Caenorhabditis elegans protein EVA-1, ...
 67-160 1.69e-16

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: 74.60  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYG---QDYQMCSSQkpaSQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGpD 143
Cdd:cd22829     6 VCEGEKLRLSCKPSSRLAIYSASYGrtlEGSVECPST---PKGDPDEECLSDVALETVMKRCHGKRRCSLTADSETFG-D 81

                          90
                  ....*....|....*...
gi 2462583019 144 LC-PGSSKYLLVSFKCQP 160
Cdd:cd22829    82 PCpPGVRKYLKVVYTCVP 99
Gal_Rha_Lectin_dCirl cd22830
galactose/rhamnose binding lectin domain found in Drosophila melanogaster Latrophilin Cirl and ...
 167-258 2.48e-16

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: 73.81  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 167 VCEDQELKLHCHESKFLNIYSATYGRRTQerDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPClP 246
Cdd:cd22830     4 ACEGSQLTLECEDGTVIRIIRANYGRFSI--AICNDHGNTDWSVNCMSPRSLRVVQERCDGKRSCSIPASSSVFGDPC-P 80

                          90
                  ....*....|..
gi 2462583019 247 GVKKYLTVTYAC 258
Cdd:cd22830    81 GTPKYLEVHYQC 92
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 167-258 3.70e-16

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: 73.49  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 167 VCEDQELKLHCHESKFLNIYSATYGRRtqERDICSSkaeRLPPF-----DCLSYSALqvLSRRCYGKQRCKIIVNNHHFG 241
Cdd:cd22835     4 ACEGSLAHLKCDEGQVISVYGADYGRR--DKTTCSF---GRPPSqiqnvECSNPTDK--VAERCNGKNSCSIKASNSVFG 76

                          90
                  ....*....|....*..
gi 2462583019 242 SPClPGVKKYLTVTYAC 258
Cdd:cd22835    77 DPC-VGTYKYLEVAYTC 92
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 163-258 3.97e-15

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: 70.78  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHChESKFLNIYSATYGRrtQERDICSSK--AERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHF 240
Cdd:cd22836     2 RTSVTCEGGYAVLKC-GSGVIQIISANYGR--TDSTTCSAGrpASQVQNTNCYASNSLAIVSQSCNGKKSCTVSASNSVF 78

                          90
                  ....*....|....*...
gi 2462583019 241 GSPClPGVKKYLTVTYAC 258
Cdd:cd22836    79 SDPC-VGTYKYLYVTYSC 95
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 62-158 5.22e-15

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: 70.52  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  62 NHTTYACDGDYLNLQCPRHSTISVQSAFYGQDYQM--CSSQ-KPASQredslTCVAATTFQKVLDECQNQRACHLLVNSR 138
Cdd:cd22840     1 ASSSVACEGDPFEISCPSGQRIKVDYASYGAIGTRstCGDSvSPAGE-----TCSAPNSLQTMRQRCQGRQSCEIRVLNS 75

                          90       100
                  ....*....|....*....|.
gi 2462583019 139 VFGPDLCPG-SSKYLLVSFKC 158
Cdd:cd22840    76 LFPNDPCPGtSKKYLEYRYRC 96
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 166-258 7.51e-14

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: 67.11  E-value: 7.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 166 TVCEDQELKLHCHESKfLNIYSATYGRrtQERDICSSkAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPCl 245
Cdd:cd22841     5 IVCEGDTDVIDCGNGV-INIHSAVYGR--TDSTTCSH-DQSVSNTNCHSDDSVNILSACCNGQSQCTVTATNSIFGDPC- 79

                          90
                  ....*....|...
gi 2462583019 246 PGVKKYLTVTYAC 258
Cdd:cd22841    80 PGTYKYLNVTYTC 92
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 68-158 1.62e-13

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: 65.91  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  68 CDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSsqkPASQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCP 146
Cdd:cd22839     7 CEGDVANLSCPEGKYISIRLANYGRfSLGVCN---PSNNIDLSTTCQNDKTLPILQKSCDGKSECSFVVSNKFFFEDPCP 83

                          90
                  ....*....|..
gi 2462583019 147 GSSKYLLVSFKC 158
Cdd:cd22839    84 GTPKYLEATYSC 95
Gal_Rha_Lectin_LAT2 cd22840
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 164-258 4.28e-13

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: 64.74  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 164 NKTVCEDQELKLHCHESKFLNIYSATYGRRTQeRDICSSkAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHF-GS 242
Cdd:cd22840     3 SSVACEGDPFEISCPSGQRIKVDYASYGAIGT-RSTCGD-SVSPAGETCSAPNSLQTMRQRCQGRQSCEIRVLNSLFpND 80

                          90
                  ....*....|....*.
gi 2462583019 243 PCLPGVKKYLTVTYAC 258
Cdd:cd22840    81 PCPGTSKKYLEYRYRC 96
Gal_Rha_Lectin_nemgal cd22838
galactose/rhamnose binding lectin domain found in Hydra vulgaris nematogalectin and similar ...
 163-260 1.10e-12

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: 63.83  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQErdICSSKAERLP---PFDCLSYSALQVLSRRCYGKQRCKIIVNNHH 239
Cdd:cd22838     2 NTAIACEGEKLWLQCPQYELIKIKSAFWGRDDKK--TCPHPPPGLPsnkMCETDEENVKKKVNDQCQGEQACEVVASNIF 79

                          90       100
                  ....*....|....*....|.
gi 2462583019 240 FGSPCLPGVKKYLTVTYACVP 260
Cdd:cd22838    80 FDDTICPDVYKYLKVKYECIP 100
Gal_Rha_Lectin_SML_rpt2 cd22835
second galactose/rhamnose binding lectin domain found in Scomberomorus niphonius ...
 67-158 1.41e-12

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: 63.47  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSSQKPASQREDSlTCvaATTFQKVLDECQNQRACHLLVNSRVFGpDLC 145
Cdd:cd22835     4 ACEGSLAHLKCDEGQVISVYGADYGRrDKTTCSFGRPPSQIQNV-EC--SNPTDKVAERCNGKNSCSIKASNSVFG-DPC 79

                          90
                  ....*....|...
gi 2462583019 146 PGSSKYLLVSFKC 158
Cdd:cd22835    80 VGTYKYLEVAYTC 92
Gal_Rha_Lectin_RBL_rpt2 cd22836
second galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding ...
 64-158 3.63e-12

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: 62.30  E-value: 3.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  64 TTYACDGDYLNLQCpRHSTISVQSAFYGQ-DYQMCSSQKPASQREDSlTCVAATTFQKVLDECQNQRACHLLVNSRVFGp 142
Cdd:cd22836     3 TSVTCEGGYAVLKC-GSGVIQIISANYGRtDSTTCSAGRPASQVQNT-NCYASNSLAIVSQSCNGKKSCTVSASNSVFS- 79

                          90
                  ....*....|....*.
gi 2462583019 143 DLCPGSSKYLLVSFKC 158
Cdd:cd22836    80 DPCVGTYKYLYVTYSC 95
Gal_Rha_Lectin_LAT1 cd22839
galactose/rhamnose binding lectin domain found in Caenorhabditis elegans latrophilin-like ...
 163-258 3.83e-12

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: 62.05  E-value: 3.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 163 KNKTVCEDQELKLHCHESKFLNIYSATYGRRTQErdICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNH-HFG 241
Cdd:cd22839     2 SSVIICEGDVANLSCPEGKYISIRLANYGRFSLG--VCNPSNNIDLSTTCQNDKTLPILQKSCDGKSECSFVVSNKfFFE 79

                          90
                  ....*....|....*..
gi 2462583019 242 SPClPGVKKYLTVTYAC 258
Cdd:cd22839    80 DPC-PGTPKYLEATYSC 95
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 168-258 6.33e-12

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: 61.35  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 168 CEDQELKLHCHESKfLNIYSATYGRRtqERDICSS--KAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPCL 245
Cdd:cd22832     6 CEGSDAQLDCDGGK-IRIQRANYGRR--DHDVCSIgrPANQLTNTNCLSQSTTSKMAERCDGKSQCIVPASNSVFGDPCV 82

                          90
                  ....*....|...
gi 2462583019 246 pGVKKYLTVTYAC 258
Cdd:cd22832    83 -GTYKYLDVAYTC 94
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 162-260 1.19e-11

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: 60.84  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 162 LKNKTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFG 241
Cdd:cd22844     1 MRRELACEGYPIELRCPGSDVIMVENANYGR--TDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFP 78

                          90
                  ....*....|....*....
gi 2462583019 242 SPClPGVKKYLTVTYACVP 260
Cdd:cd22844    79 DPC-PGTYKYLEVQYDCVP 96
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
 64-158 1.96e-11

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: 60.16  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  64 TTYACDGDYLNLQCpRHSTISVQSAFYGQ-DYQMCSSQKPASQREDSlTCVAATTFQKVLDECQNQRACHLLVNSRVFGP 142
Cdd:cd22834     4 TSITCEGSPVSLDC-GPDVIKIYDANYGRrDSTTCSHGRPESQLTNT-NCYLPETTKVMSERCNGKSLCDLLASNVVTDP 81

                          90
                  ....*....|....*.
gi 2462583019 143 dlCPGSSKYLLVSFKC 158
Cdd:cd22834    82 --CYGTYKYLEVSYSC 95
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 68-158 2.23e-11

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: 59.75  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  68 CDGDYLNLQCpRHSTISVQSAFYGQ-DYQMCSSQKPASqredslTCVAATTFQKVLDECQNQRACHLLVNSRVFGpDLCP 146
Cdd:cd22837     4 CENDSATITC-SPETINVISAFYGRtDSTTCSHGRPST------TNCSSDTLAYIRALCQGKQTCTLQASNSVFG-DPCP 75

                          90
                  ....*....|..
gi 2462583019 147 GSSKYLLVSFKC 158
Cdd:cd22837    76 GTYKYLRITYSC 87
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
 162-260 4.14e-11

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: 59.34  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 162 LKNKTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFG 241
Cdd:cd22846     2 VRRELSCESYPIELRCPGTDVIMIESANYGR--TDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFP 79

                          90
                  ....*....|....*....
gi 2462583019 242 SPClPGVKKYLTVTYACVP 260
Cdd:cd22846    80 DPC-PGTYKYLEVQYECVP 97
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
 166-260 4.24e-11

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: 59.20  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 166 TVCEDQEL-KLHChESKFLNIYSATYGRRtqERDICSS--KAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGS 242
Cdd:cd22833     4 TTCDGNNVhRLSC-DTGVINVQSALYGRT--DSETCSEgrPPEQLTNTQCSQSGTLDLLKNRCDGKKVCELNTNDFRTSD 80

                          90
                  ....*....|....*...
gi 2462583019 243 PClPGVKKYLTVTYACVP 260
Cdd:cd22833    81 PC-PGTYKYLQTNYTCLP 97
Gal_Rha_Lectin_CSL1-2_RBL_SML_rpt1 cd22833
first galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1-2, Silurus ...
 68-160 1.46e-10

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: 57.66  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  68 CDGDYLN-LQCpRHSTISVQSAFYGQ-DYQMCSSQKPASQREDSlTCVAATTFQKVLDECQNQRACHLlvNSRVFG-PDL 144
Cdd:cd22833     6 CDGNNVHrLSC-DTGVINVQSALYGRtDSETCSEGRPPEQLTNT-QCSQSGTLDLLKNRCDGKKVCEL--NTNDFRtSDP 81

                          90
                  ....*....|....*.
gi 2462583019 145 CPGSSKYLLVSFKCQP 160
Cdd:cd22833    82 CPGTYKYLQTNYTCLP 97
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 168-260 3.27e-10

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: 56.94  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 168 CEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSPClPG 247
Cdd:cd22845     7 CEGYPIDLRCPGSDVIMIESANYGR--TDDKICDADPFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVFPDPC-PG 83

                          90
                  ....*....|...
gi 2462583019 248 VKKYLTVTYACVP 260
Cdd:cd22845    84 TYKYLEVQYECVP 96
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 69-158 4.86e-10

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: 56.14  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  69 DGDYLNLQCPRHSTIS-VQSAFYGQDYQMCSSQKPAsqredslTCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCPG 147
Cdd:cd22842     8 PGSTLTLSCPAGQVISsIDFASYGTPTGTCGSFSKG-------SCHAPNSLSVVEKACLGKNSCSIPASNSVFFGDPCPG 80

                          90
                  ....*....|.
gi 2462583019 148 SSKYLLVSFKC 158
Cdd:cd22842    81 TTKRLAVQATC 91
Gal_Rha_Lectin_CSL3_rpt1_rpt2-like cd22832
first and second galactose/rhamnose binding lectin domain found in Oncorhynchus keta ...
 64-158 1.69e-09

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


Pssm-ID: 438689 [Multi-domain]  Cd Length: 94  Bit Score: 54.80  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  64 TTYACDGDYLNLQCPRhSTISVQSAFYGQ-DYQMCSSQKPASQREDsLTCVAATTFQKVLDECQNQRACHLLVNSRVFGp 142
Cdd:cd22832     2 SSITCEGSDAQLDCDG-GKIRIQRANYGRrDHDVCSIGRPANQLTN-TNCLSQSTTSKMAERCDGKSQCIVPASNSVFG- 78

                          90
                  ....*....|....*.
gi 2462583019 143 DLCPGSSKYLLVSFKC 158
Cdd:cd22832    79 DPCVGTYKYLDVAYTC 94
Gal_Rha_Lectin_RBL_rpt3 cd22837
third galactose/rhamnose binding lectin domain found in Silurus asotus rhamnose-binding lectin ...
 166-258 1.70e-09

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: 54.35  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 166 TVCEDQELKLHChESKFLNIYSATYGRrtQERDICSSKaeRLPPFDCLSYSALQVLSRrCYGKQRCKIIVNNHHFGSPCl 245
Cdd:cd22837     2 IICENDSATITC-SPETINVISAFYGR--TDSTTCSHG--RPSTTNCSSDTLAYIRAL-CQGKQTCTLQASNSVFGDPC- 74

                          90
                  ....*....|...
gi 2462583019 246 PGVKKYLTVTYAC 258
Cdd:cd22837    75 PGTYKYLRITYSC 87
Gal_Rha_Lectin_LPHN2 cd22845
galactose/rhamnose binding lectin domain found in latrophilin-2 and similar proteins; ...
 67-160 1.95e-09

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: 54.63  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSSQkpaSQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFgPDLC 145
Cdd:cd22845     6 SCEGYPIDLRCPGSDVIMIESANYGRtDDKICDAD---PFQMENTDCYLPDAYKIMTQRCNNRTQCIVVTGSDVF-PDPC 81

                          90
                  ....*....|....*
gi 2462583019 146 PGSSKYLLVSFKCQP 160
Cdd:cd22845    82 PGTYKYLEVQYECVP 96
Gal_Rha_Lectin_LPHN1 cd22844
galactose/rhamnose binding lectin domain found in latrophilin-1 and similar proteins; ...
 67-160 2.49e-09

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: 54.29  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSSQkpaSQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFgPDLC 145
Cdd:cd22844     6 ACEGYPIELRCPGSDVIMVENANYGRtDDKICDAD---PFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAF-PDPC 81

                          90
                  ....*....|....*
gi 2462583019 146 PGSSKYLLVSFKCQP 160
Cdd:cd22844    82 PGTYKYLEVQYDCVP 96
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
 167-258 3.76e-09

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: 53.89  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 167 VCEDQELKLHCHESKFLNIYSATYGRRTqeRDICSSKAERLPPF---DCLSYSALQVLSRRCYGKQRCKIIVNNHHFGSP 243
Cdd:cd22831     5 ACEDYNATLQCGSGQVIEIDDSFYGRNT--PHYCRSENPSPPTDsqeRCSWVDVRDLVAAQCHGLQVCQIPADPSSFGEP 82

                          90
                  ....*....|....*
gi 2462583019 244 ClPGVKKYLTVTYAC 258
Cdd:cd22831    83 C-PELGSYLSVEYHC 96
Gal_Rha_Lectin_LPHN3 cd22846
galactose/rhamnose binding lectin domain found in latrophilin-3 and similar proteins; ...
 67-160 8.29e-09

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: 52.80  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  67 ACDGDYLNLQCPRHSTISVQSAFYGQ-DYQMCSSQkPAsQREDSlTCVAATTFQKVLDECQNQRACHLLVNSRVFgPDLC 145
Cdd:cd22846     7 SCESYPIELRCPGTDVIMIESANYGRtDDKICDSD-PA-QMENI-RCYLPDAYKIMSQRCNNRTQCAVVAGPDVF-PDPC 82

                          90
                  ....*....|....*
gi 2462583019 146 PGSSKYLLVSFKCQP 160
Cdd:cd22846    83 PGTYKYLEVQYECVP 97
Gal_Rha_Lectin_CSL1_rpt2 cd22834
second galactose/rhamnose binding lectin domain found in Oncorhynchus keta CSL1 and similar ...
 168-258 1.09e-08

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: 52.46  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 168 CEDQELKLHCHESkFLNIYSATYGRRtqERDICSSK--AERLPPFDCLSYSALQVLSRRCYGKQRCKIIVNNhHFGSPCL 245
Cdd:cd22834     8 CEGSPVSLDCGPD-VIKIYDANYGRR--DSTTCSHGrpESQLTNTNCYLPETTKVMSERCNGKSLCDLLASN-VVTDPCY 83

                          90
                  ....*....|...
gi 2462583019 246 pGVKKYLTVTYAC 258
Cdd:cd22834    84 -GTYKYLEVSYSC 95
Gal_Rha_Lectin_REJ3 cd22841
galactose/rhamnose binding lectin domain found in Strongylocentrotus purpuratus receptor for ...
 68-158 2.95e-08

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: 50.93  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  68 CDGDYLNLQCPrHSTISVQSAFYGQ-DYQMCSSQKPASQRedslTCVAATTFQKVLDECQNQRACHLLVNSRVFGpDLCP 146
Cdd:cd22841     7 CEGDTDVIDCG-NGVINIHSAVYGRtDSTTCSHDQSVSNT----NCHSDDSVNILSACCNGQSQCTVTATNSIFG-DPCP 80

                          90
                  ....*....|..
gi 2462583019 147 GSSKYLLVSFKC 158
Cdd:cd22841    81 GTYKYLNVTYTC 92
Gal_Rha_Lectin_PKD1L2 cd22831
galactose binding lectin domain found in polycystic kidney disease protein 1-like 2 ...
 65-158 1.54e-06

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: 46.19  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  65 TYACDGDYLNLQCPRHSTISVQSAFYG-QDYQMCSSQKPASQREDSLTCVAATTFQKVLDECQNQRACHLLVNSRVFGpD 143
Cdd:cd22831     3 SLACEDYNATLQCGSGQVIEIDDSFYGrNTPHYCRSENPSPPTDSQERCSWVDVRDLVAAQCHGLQVCQIPADPSSFG-E 81

                          90
                  ....*....|....*
gi 2462583019 144 LCPGSSKYLLVSFKC 158
Cdd:cd22831    82 PCPELGSYLSVEYHC 96
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 162-258 5.30e-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: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 162 LKNKTVCEDQELKLHCHESKFLNIYSATYGRrtQERDICSSKAERLPPFDCLSYsalqvLSRRCYGKQRCKIIVNNHHFG 241
Cdd:cd22843     1 PHTAFVCFGQEVTIHCPGDGNISIKSATYGY--NNSNVCIYCNSFNCDKDITSP-----VNKKCCGKNTCVLTVSDILEG 73

                          90
                  ....*....|....*..
gi 2462583019 242 SPClPGVKKYLTVTYAC 258
Cdd:cd22843    74 NPC-GIGNSYIRVVYTC 89
Gal_Rha_Lectin_BGal cd22842
galactose/rhamnose binding lectin domain found in plant beta-galactosidases and similar ...
 212-258 1.07e-05

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: 43.81  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462583019 212 CLSYSALQVLSRRCYGKQRCKIIVNN-HHFGSPClPGVKKYLTVTYAC 258
Cdd:cd22842    45 CHAPNSLSVVEKACLGKNSCSIPASNsVFFGDPC-PGTTKRLAVQATC 91
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 63-158 1.58e-05

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: 43.20  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  63 HTTYACDGDYLNLQCPRHSTISVQSAFYGQDyqmcssqkPASQREDSLTCVAATTFQK-VLDECQNQRACHLLVNSrVFG 141
Cdd:cd22843     2 HTAFVCFGQEVTIHCPGDGNISIKSATYGYN--------NSNVCIYCNSFNCDKDITSpVNKKCCGKNTCVLTVSD-ILE 72

                          90
                  ....*....|....*..
gi 2462583019 142 PDLCPGSSKYLLVSFKC 158
Cdd:cd22843    73 GNPCGIGNSYIRVVYTC 89
PLN03059 PLN03059
beta-galactosidase; Provisional
 74-158 3.60e-05

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 46.15  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019  74 NLQCPRHSTIS-VQSAFYGQDYQMCSSQKPASqredsltCVAATTFQKVLDECQNQRACHLLVNSRVFGPDLCPGSSKYL 152
Cdd:PLN03059  761 HLWCPPGQKISkIKFASFGVPQGTCGSFREGS-------CHAHKSYDAFERNCIGKQSCSVTVAPEVFGGDPCPDSMKKL 833


                  ....*.
gi 2462583019 153 LVSFKC 158
Cdd:PLN03059  834 SVEAVC 839
PLN03059 PLN03059
beta-galactosidase; Provisional
 156-258 7.15e-04

beta-galactosidase; Provisional


Pssm-ID: 166698 [Multi-domain]  Cd Length: 840  Bit Score: 41.91  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462583019 156 FKCQPKLKN-------KTVCEDQELKLHC-HESKFLNIYSATYGrrtQERDICSSKAERlppfDCLSYSALQVLSRRCYG 227
Cdd:PLN03059  736 FEGQPALKNwqiiasgKVNSLQPKAHLWCpPGQKISKIKFASFG---VPQGTCGSFREG----SCHAHKSYDAFERNCIG 808

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462583019 228 KQRCKIIVNNHHF-GSPClPGVKKYLTVTYAC 258
Cdd:PLN03059  809 KQSCSVTVAPEVFgGDPC-PDSMKKLSVEAVC 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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