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Conserved domains on  [gi|597517899|ref|NP_001277986|]
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galectin-8 isoform 3 [Mus musculus]

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 ...
101-220 3.02e-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: 146.58  E-value: 3.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899   101 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 180
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 597517899   181 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 220
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
1-55 5.28e-17

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: 73.78  E-value: 5.28e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899     1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
101-220 3.02e-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: 146.58  E-value: 3.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899   101 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 180
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 597517899   181 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 220
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
92-217 1.79e-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: 139.69  E-value: 1.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899  92 PFEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKTrDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 171
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 597517899 172 YFEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRL 217
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
101-220 2.83e-41

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: 136.62  E-value: 2.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899  101 MGPGRTVVIKGEVNTNARSFNVDLVAG--KTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 178
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 597517899  179 CDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 220
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
1-55 5.28e-17

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: 73.78  E-value: 5.28e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899     1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
1-55 5.60e-16

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: 71.51  E-value: 5.60e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899   1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:cd00070   72 FPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
1-55 6.53e-16

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: 71.13  E-value: 6.53e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899    1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:pfam00337  69 FPFQPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
101-220 3.02e-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: 146.58  E-value: 3.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899   101 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 180
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 597517899   181 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 220
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
92-217 1.79e-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: 139.69  E-value: 1.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899  92 PFEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKTrDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 171
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 597517899 172 YFEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRL 217
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
93-221 2.82e-41

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 136.97  E-value: 2.82e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899    93 FEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKtRDIALHLNPRLNVKAFVRNSFLQDAWGEEERnITCFPFSSGMY 172
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGG-DDIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQPGQP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 597517899   173 FEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDVR 221
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
101-220 2.83e-41

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: 136.62  E-value: 2.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517899  101 MGPGRTVVIKGEVNTNARSFNVDLVAG--KTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 178
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 597517899  179 CDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 220
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
1-55 5.28e-17

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: 73.78  E-value: 5.28e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899     1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
1-55 5.60e-16

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: 71.51  E-value: 5.60e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899   1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:cd00070   72 FPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
1-55 6.53e-16

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: 71.13  E-value: 6.53e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 597517899    1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 55
Cdd:pfam00337  69 FPFQPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
1-57 1.02e-12

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 62.63  E-value: 1.02e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 597517899     1 MPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSIGF 57
Cdd:smart00276  71 FPFQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 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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