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Conserved domains on  [gi|156151366|ref|NP_054900|]
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galectin-related protein [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 ...
 46-170 5.05e-45

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: 144.27  E-value: 5.05e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366    46 GGMRPGKKVLVMGIVDLNPESFAISLTCGdsedPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAiPYFPFIPDQPFR 125
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 156151366   126 VEILCEHPRFRVFVDGHQLFDFYHRIqTLSAIDTIKINGDLQITK 170
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTS 120
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 46-170 5.05e-45

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: 144.27  E-value: 5.05e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366    46 GGMRPGKKVLVMGIVDLNPESFAISLTCGdsedPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAiPYFPFIPDQPFR 125
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 156151366   126 VEILCEHPRFRVFVDGHQLFDFYHRIqTLSAIDTIKINGDLQITK 170
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTS 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 39-171 3.26e-37

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: 124.67  E-value: 3.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366  39 PFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSedppaDVAIELKAVFTDRQLLRNSCISGERGEEQSAiPYFPF 118
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156151366 119 IPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQtLSAIDTIKINGDLQITKL 171
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 46-171 8.30e-36

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: 120.82  E-value: 8.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366   46 GGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPpaDVAIELKAVFTDRQLLRNSCISGERGEEQSaIPYFPFIPDQPFR 125
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSD--DIALHFNPRFDENVIVRNSRQNGQWGQEER-EGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156151366  126 VEILCEHPRFRVFVDGHQLFDFYHRIQtLSAIDTIKINGDLQITKL 171
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 46-170 5.05e-45

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: 144.27  E-value: 5.05e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366    46 GGMRPGKKVLVMGIVDLNPESFAISLTCGdsedPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAiPYFPFIPDQPFR 125
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 156151366   126 VEILCEHPRFRVFVDGHQLFDFYHRIqTLSAIDTIKINGDLQITK 170
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTS 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 39-171 3.26e-37

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: 124.67  E-value: 3.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366  39 PFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSedppaDVAIELKAVFTDRQLLRNSCISGERGEEQSAiPYFPF 118
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156151366 119 IPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQtLSAIDTIKINGDLQITKL 171
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 46-171 8.30e-36

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: 120.82  E-value: 8.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366   46 GGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPpaDVAIELKAVFTDRQLLRNSCISGERGEEQSaIPYFPFIPDQPFR 125
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSD--DIALHFNPRFDENVIVRNSRQNGQWGQEER-EGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156151366  126 VEILCEHPRFRVFVDGHQLFDFYHRIQtLSAIDTIKINGDLQITKL 171
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 43-171 2.95e-23

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 88.82  E-value: 2.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156151366    43 HIKGGMRPGKKVLVMGIVDLNPESFAISLTCGdsedpPADVAIELKAVFTDRQLLRNSCISGERGEEQSaIPYFPFIPDQ 122
Cdd:smart00276   4 PIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG-----GDDIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQPGQ 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 156151366   123 PFRVEILCEHPRFRVFVDGHQLFDFYHRIQtLSAIDTIKINGDLQITKL 171
Cdd:smart00276  78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSV 125
 
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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