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Conserved domains on  [gi|2462528347|ref|XP_054226284|]
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galectin-12 isoform X2 [Homo sapiens]

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 ...
 55-181 2.54e-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: 145.04  E-value: 2.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347   55 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 134
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462528347  135 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 55-181 2.54e-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: 145.04  E-value: 2.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347   55 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 134
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462528347  135 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 48-181 6.98e-43

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: 6.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347  48 PYVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHL 127
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNA-KRFSINLGTGSS-----DIALHFNPRFD--ENVIVRNSFLNGNWGPEERSGGF 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528347 128 ALRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:cd00070    73 PFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 55-181 1.01e-40

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: 135.85  E-value: 1.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347  55 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSS 134
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQ-RFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462528347 135 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:pfam00337  77 FELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 55-181 2.54e-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: 145.04  E-value: 2.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347   55 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 134
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462528347  135 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 48-181 6.98e-43

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: 6.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347  48 PYVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHL 127
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNA-KRFSINLGTGSS-----DIALHFNPRFD--ENVIVRNSFLNGNWGPEERSGGF 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528347 128 ALRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:cd00070    73 PFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 55-181 1.01e-40

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: 135.85  E-value: 1.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347  55 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSS 134
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQ-RFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462528347 135 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 181
Cdd:pfam00337  77 FELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 49-183 2.05e-31

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 111.94  E-value: 2.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528347   49 YVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLA 128
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDA-KRFSINLLTGGD-----DIALHFNPRFN--ENKIVCNSKLNGSWGSEEREGGFP 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462528347  129 LRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAVGF 183
Cdd:smart00276  73 FQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 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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