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Conserved domains on  [gi|1935010081|ref|NP_001375428|]
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galectin-9 isoform 1 [Rattus norvegicus]

Protein Classification

galectin family protein( domain architecture ID 10658251)

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 ...
 231-353 5.97e-53

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: 170.85  E-value: 5.97e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  231 PNGFYPSKSINISGVVLPDAKRFHINLRCG--GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQSFSVW 308
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1935010081  309 ILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-145 2.30e-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: 161.60  E-value: 2.30e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081   22 QGGLQNGLQITLQGTVHPFPNRIAVNFQTGfSGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGMPFELC 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG-PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1935010081  102 FLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFIN 145
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 231-353 5.97e-53

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: 170.85  E-value: 5.97e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  231 PNGFYPSKSINISGVVLPDAKRFHINLRCG--GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQSFSVW 308
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1935010081  309 ILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 225-353 2.85e-51

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: 166.66  E-value: 2.85e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081 225 PFFTSIPNGFYPSKSINISGVVLPDAKRFHINLRCG-GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQ 303
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1935010081 304 SFSVWILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:cd00070    79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-145 2.30e-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: 161.60  E-value: 2.30e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081   22 QGGLQNGLQITLQGTVHPFPNRIAVNFQTGfSGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGMPFELC 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG-PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1935010081  102 FLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFIN 145
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-144 3.23e-48

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: 158.95  E-value: 3.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  16 PFTGIIQGGLQNGLQITLQGTVHPFPNRIAVNFQTGfsGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKG 95
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG--SSDIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1935010081  96 MPFELCFLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFI 144
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 231-353 1.07e-46

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: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081 231 PNGFYPSKSINISGVVLPDAKRFHINLRCG----GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSLPgrMPFNRGQSFS 306
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG--FPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1935010081 307 VWILCEGHCFKVAVDGQHICEYYHRLKNlPDINTLEVAGDIQLTHVQ 353
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-145 1.16e-42

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: 144.32  E-value: 1.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  22 QGGLQNGLQITLQGTVHPFPNRIAVNFQTG-FSGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGMPFEL 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvGPSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1935010081 101 CFLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFIN 145
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 231-353 5.97e-53

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: 170.85  E-value: 5.97e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  231 PNGFYPSKSINISGVVLPDAKRFHINLRCG--GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQSFSVW 308
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1935010081  309 ILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 225-353 2.85e-51

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: 166.66  E-value: 2.85e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081 225 PFFTSIPNGFYPSKSINISGVVLPDAKRFHINLRCG-GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQ 303
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1935010081 304 SFSVWILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:cd00070    79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-145 2.30e-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: 161.60  E-value: 2.30e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081   22 QGGLQNGLQITLQGTVHPFPNRIAVNFQTGfSGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGMPFELC 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG-PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1935010081  102 FLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFIN 145
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-144 3.23e-48

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: 158.95  E-value: 3.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  16 PFTGIIQGGLQNGLQITLQGTVHPFPNRIAVNFQTGfsGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKG 95
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG--SSDIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1935010081  96 MPFELCFLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFI 144
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 226-353 3.38e-48

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 158.93  E-value: 3.38e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  226 FFTSIPNGFYPSKSINISGVVLPDAKRFHINLRCGG-DIAFHLNPRFNEKVVVRNTQINNSWGPEERSlpGRMPFNRGQS 304
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGdDIALHFNPRFNENKIVCNSKLNGSWGSEERE--GGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1935010081  305 FSVWILCEGHCFKVAVDGQHICEYYHRLKnLPDINTLEVAGDIQLTHVQ 353
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 231-353 1.07e-46

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: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081 231 PNGFYPSKSINISGVVLPDAKRFHINLRCG----GDIAFHLNPRFNEKVVVRNTQINNSWGPEERSLPgrMPFNRGQSFS 306
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG--FPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1935010081 307 VWILCEGHCFKVAVDGQHICEYYHRLKNlPDINTLEVAGDIQLTHVQ 353
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 17-146 3.52e-43

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 145.83  E-value: 3.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081   17 FTGIIQGGLQNGLQITLQGTVHPFPNRIAVNFQTGfsGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGM 96
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG--GDDIALHFNPRFNEN-KIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1935010081   97 PFELCFLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFINF 146
Cdd:smart00276  78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-145 1.16e-42

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: 144.32  E-value: 1.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935010081  22 QGGLQNGLQITLQGTVHPFPNRIAVNFQTG-FSGNDIAFHFNPRFEEGgYVVCNTKQNGKWGPEERKMQMPFQKGMPFEL 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvGPSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1935010081 101 CFLVQRSEFKVMVNKNFFVQYSHRVPYHLVDTISVSGCLHLSFIN 145
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
 
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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