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Conserved domains on  [gi|1664160185|ref|NP_001357615|]
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galectin-12 isoform 2 [Mus musculus]

Protein Classification

GLECT domain-containing protein( domain architecture ID 10448431)

GLECT domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-158 3.69e-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: 149.33  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  33 GGLYAGKMVTLQGVVPLHARRFQVDFQCGccLHPQPDVAFRFSPRFYtvKPHVICNTHQGGLWQKEIRWPGVALQRGDSF 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFD--ENVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 113 LILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 182-300 2.01e-20

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: 84.56  E-value: 2.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  182 PRGLWPGQVIVVRGLVLKEPKDFTLSL-KDGTTHVPVTLRASFTDRTL---AWVS-SWGRKKlISAPFLFHPQRFFEVLL 256
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLqCGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664160185  257 LCQEGGLKLALNGQGLGATSLdQKALEQLRELRISGNVHLYCVH 300
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPH-RLPLESIDTLEISGDVQLTSVQ 122
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-158 3.69e-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: 149.33  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  33 GGLYAGKMVTLQGVVPLHARRFQVDFQCGccLHPQPDVAFRFSPRFYtvKPHVICNTHQGGLWQKEIRWPGVALQRGDSF 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFD--ENVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 113 LILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 33-158 1.51e-44

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: 147.74  E-value: 1.51e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185   33 GGLYAGKMVTLQGVVPLHARRFQVDFQCGcclhPQPDVAFRFSPRFytVKPHVICNTHQGGLWQKEIRWPGVALQRGDSF 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRF--DEGTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1664160185  113 LILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-158 4.15e-42

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: 141.62  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  26 PYGTTIFGGLYAGKMVTLQGVVPLHARRFQVDFQCGcclhpQPDVAFRFSPRFytVKPHVICNTHQGGLWQKEIRWPGVA 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG-----SSDIALHFNPRF--DENVIVRNSFLNGNWGPEERSGGFP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1664160185 106 LQRGDSFLILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:cd00070    74 FQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 182-300 2.01e-20

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: 84.56  E-value: 2.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  182 PRGLWPGQVIVVRGLVLKEPKDFTLSL-KDGTTHVPVTLRASFTDRTL---AWVS-SWGRKKlISAPFLFHPQRFFEVLL 256
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLqCGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664160185  257 LCQEGGLKLALNGQGLGATSLdQKALEQLRELRISGNVHLYCVH 300
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPH-RLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 180-300 7.26e-08

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: 50.33  E-value: 7.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185 180 ALPRGLWPGQVIVVRGLVLKEPKDFTLSLKDGTTHVPVTLRASFTDRTL---AWVS-SWGRKKlISAPFLFHPQRFFEVL 255
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 256 LLCQEGGLKLALNGQGLgaTSLDQKA-LEQLRELRISGNVHLYCVH 300
Cdd:cd00070    84 ILVEEDKFQIFVNGQHF--FSFPHRLpLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 182-300 7.85e-07

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: 47.25  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185 182 PRGLWPGQVIVVRGLVLKEPKDFTLSLKDG---TTHVPVTLRASFTDRTL---AWVS-SWGRkKLISAPFLFHPQRFFEV 254
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpSDDIALHFNPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 255 LLLCQEGGLKLALNGQgLGATSLDQKALEQLRELRISGNVHLYCVH 300
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-158 3.69e-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: 149.33  E-value: 3.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  33 GGLYAGKMVTLQGVVPLHARRFQVDFQCGccLHPQPDVAFRFSPRFYtvKPHVICNTHQGGLWQKEIRWPGVALQRGDSF 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFD--ENVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 113 LILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 33-158 1.51e-44

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: 147.74  E-value: 1.51e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185   33 GGLYAGKMVTLQGVVPLHARRFQVDFQCGcclhPQPDVAFRFSPRFytVKPHVICNTHQGGLWQKEIRWPGVALQRGDSF 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRF--DEGTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1664160185  113 LILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-158 4.15e-42

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: 141.62  E-value: 4.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  26 PYGTTIFGGLYAGKMVTLQGVVPLHARRFQVDFQCGcclhpQPDVAFRFSPRFytVKPHVICNTHQGGLWQKEIRWPGVA 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG-----SSDIALHFNPRF--DENVIVRNSFLNGNWGPEERSGGFP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1664160185 106 LQRGDSFLILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAV 158
Cdd:cd00070    74 FQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 27-160 5.08e-30

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 110.01  E-value: 5.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185   27 YGTTIFGGLYAGKMVTLQGVVPLHARRFQVDFQCGcclhpQPDVAFRFSPRFYtvKPHVICNTHQGGLWQKEIRWPGVAL 106
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG-----GDDIALHFNPRFN--ENKIVCNSKLNGSWGSEEREGGFPF 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1664160185  107 QRGDSFLILFLFENEEVKVSVNGQHFLHYRYRLPLSRVDTLDISGDILVKAVGF 160
Cdd:smart00276  74 QPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 182-300 2.01e-20

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: 84.56  E-value: 2.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  182 PRGLWPGQVIVVRGLVLKEPKDFTLSL-KDGTTHVPVTLRASFTDRTL---AWVS-SWGRKKlISAPFLFHPQRFFEVLL 256
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLqCGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664160185  257 LCQEGGLKLALNGQGLGATSLdQKALEQLRELRISGNVHLYCVH 300
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPH-RLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 180-300 7.26e-08

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: 50.33  E-value: 7.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185 180 ALPRGLWPGQVIVVRGLVLKEPKDFTLSLKDGTTHVPVTLRASFTDRTL---AWVS-SWGRKKlISAPFLFHPQRFFEVL 255
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 256 LLCQEGGLKLALNGQGLgaTSLDQKA-LEQLRELRISGNVHLYCVH 300
Cdd:cd00070    84 ILVEEDKFQIFVNGQHF--FSFPHRLpLESIDYLSINGDVSLTSVE 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 179-300 7.37e-08

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 50.30  E-value: 7.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185  179 RALPRGLWPGQVIVVRGLVLKEPKDFTLSLKDGTTHVPVTLRASFTDRTL---AWV-SSWGRKKLISApFLFHPQRFFEV 254
Cdd:smart00276   3 LPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGDDIALHFNPRFNENKIvcnSKLnGSWGSEEREGG-FPFQPGQPFDL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1664160185  255 LLLCQEGGLKLALNGQGLgaTSLDQKA-LEQLRELRISGNVHLYCVH 300
Cdd:smart00276  82 TIIVQPDHFQIFVNGVHI--TTFPHRLpLESIDYLSINGDVQLTSVS 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 182-300 7.85e-07

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: 47.25  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664160185 182 PRGLWPGQVIVVRGLVLKEPKDFTLSLKDG---TTHVPVTLRASFTDRTL---AWVS-SWGRkKLISAPFLFHPQRFFEV 254
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpSDDIALHFNPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664160185 255 LLLCQEGGLKLALNGQgLGATSLDQKALEQLRELRISGNVHLYCVH 300
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 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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