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Conserved domains on  [gi|4504985|ref|NP_002298|]
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galectin-7 [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 ...
 11-133 8.33e-54

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: 165.07  E-value: 8.33e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985      11 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 90
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4504985      91 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 11-133 8.33e-54

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: 165.07  E-value: 8.33e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985      11 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 90
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4504985      91 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-133 3.75e-52

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: 3.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985    5 PHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRG 84
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4504985   85 QPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 11-133 6.12e-51

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: 157.80  E-value: 6.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985     11 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 90
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4504985     91 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:pfam00337  81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 11-133 8.33e-54

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: 165.07  E-value: 8.33e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985      11 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 90
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4504985      91 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-133 3.75e-52

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: 3.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985    5 PHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRG 84
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4504985   85 QPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 7-135 3.04e-51

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 158.93  E-value: 3.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985       7 KSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQP 86
Cdd:smart00276   2 TLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG---GDDIALHFNPRFNENKIVCNSKLNGSWGSEEREGGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 4504985      87 FEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSVRI 135
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 11-133 6.12e-51

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: 157.80  E-value: 6.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504985     11 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 90
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4504985     91 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 133
Cdd:pfam00337  81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
 
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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