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Conserved domains on  [gi|226531139|ref|NP_001152773|]
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galectin-9 isoform 2 [Mus musculus]

Protein Classification

galectin family protein( domain architecture ID 10049251)

galectin family protein may exclusively bind beta-galactosides such as lactose in a manner independent of metal ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 199-321 3.24e-55

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


:

Pssm-ID: 214904  Cd Length: 122  Bit Score: 175.47  E-value: 3.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   199 PNGLYPSKSIMISGNVLPDATRFHINLRCG--GDIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQSFSVW 276
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 226531139   277 IICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-145 2.02e-49

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


:

Pssm-ID: 238025  Cd Length: 127  Bit Score: 160.88  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139  16 PFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSfnGNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKG 95
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG--SSDIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPFQPG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226531139  96 MPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFIT 145
Cdd:cd00070   78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 199-321 3.24e-55

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 175.47  E-value: 3.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   199 PNGLYPSKSIMISGNVLPDATRFHINLRCG--GDIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQSFSVW 276
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 226531139   277 IICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 193-321 8.31e-54

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 172.05  E-value: 8.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139 193 PFYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCG-GDIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQ 271
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226531139 272 SFSVWIICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-145 2.02e-49

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 160.88  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139  16 PFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSfnGNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKG 95
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG--SSDIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPFQPG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226531139  96 MPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFIT 145
Cdd:cd00070   78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-145 2.24e-49

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 160.45  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139    22 QGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFNGnDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKGMPFELC 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA-DIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 226531139   102 FLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFIT 145
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 199-321 4.03e-47

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 154.72  E-value: 4.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139  199 PNGLYPSKSIMISGNVLPDATRFHINLRCG----GDIAFHLNPRFNENAVVRNTQINNSWGQEERSLLgrMPFSRGQSFS 274
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG--FPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 226531139  275 VWIICEGHCFKVAVNGQHMCEYYHRLKNlQDINTLEVAGDIQLTHVQ 321
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-142 7.54e-45

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 148.94  E-value: 7.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   22 QGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFN-GNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKGMPFEL 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGpSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 226531139  101 CFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLS 142
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLT 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 199-321 3.24e-55

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 175.47  E-value: 3.24e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   199 PNGLYPSKSIMISGNVLPDATRFHINLRCG--GDIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQSFSVW 276
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 226531139   277 IICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 193-321 8.31e-54

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 172.05  E-value: 8.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139 193 PFYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCG-GDIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQ 271
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226531139 272 SFSVWIICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 194-321 6.56e-51

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 164.71  E-value: 6.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   194 FYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCGG-DIAFHLNPRFNENAVVRNTQINNSWGQEERSllGRMPFSRGQS 272
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGdDIALHFNPRFNENKIVCNSKLNGSWGSEERE--GGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 226531139   273 FSVWIICEGHCFKVAVNGQHMCEYYHRLKnLQDINTLEVAGDIQLTHVQ 321
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-145 2.02e-49

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 160.88  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139  16 PFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSfnGNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKG 95
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG--SSDIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPFQPG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226531139  96 MPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFIT 145
Cdd:cd00070   78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-145 2.24e-49

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 160.45  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139    22 QGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFNGnDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKGMPFELC 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA-DIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 226531139   102 FLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFIT 145
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 199-321 4.03e-47

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 154.72  E-value: 4.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139  199 PNGLYPSKSIMISGNVLPDATRFHINLRCG----GDIAFHLNPRFNENAVVRNTQINNSWGQEERSLLgrMPFSRGQSFS 274
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG--FPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 226531139  275 VWIICEGHCFKVAVNGQHMCEYYHRLKNlQDINTLEVAGDIQLTHVQ 321
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-142 7.54e-45

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 148.94  E-value: 7.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139   22 QGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFN-GNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKGMPFEL 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGpSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 226531139  101 CFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLS 142
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLT 121
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 17-146 1.31e-44

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 148.53  E-value: 1.31e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226531139    17 FTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSfnGNDIAFHFNPRFEEGgYVVCNTKQNGQWGPEERKMQMPFQKGM 96
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG--GDDIALHFNPRFNEN-KIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 226531139    97 PFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFITF 146
Cdd:smart00276  78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
 
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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