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Conserved domains on  [gi|3891481]
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Chain A, Galectin-7

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 ...
 10-132 1.24e-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: 164.69  E-value: 1.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481      10 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 3891481      90 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
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 ...
 10-132 1.24e-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: 164.69  E-value: 1.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481      10 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 3891481      90 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 4-132 4.74e-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: 4.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481    4 PHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRG 83
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 3891481   84 QPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 10-132 9.54e-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: 157.42  E-value: 9.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481     10 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 89
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 3891481     90 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
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 ...
 10-132 1.24e-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: 164.69  E-value: 1.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481      10 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 3891481      90 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
Cdd:smart00908  79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 4-132 4.74e-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: 4.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481    4 PHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRG 83
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 3891481   84 QPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 6-134 4.79e-51

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 158.16  E-value: 4.79e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481       6 KSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGeeqGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQP 85
Cdd:smart00276   2 TLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG---GDDIALHFNPRFNENKIVCNSKLNGSWGSEEREGGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 3891481      86 FEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSVRI 134
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 10-132 9.54e-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: 157.42  E-value: 9.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3891481     10 PEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVL 89
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 3891481     90 IIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSV 132
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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