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Conserved domains on  [gi|564391995|ref|XP_006254230|]
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galectin-8 isoform X1 [Rattus norvegicus]

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 ...
 24-148 2.08e-49

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: 160.45  E-value: 2.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995    24 EQLKPGSLIVIRGHVPKDSERFQVDFQHGnslkPRADVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 564391995   104 IVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 194-313 8.81e-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: 148.51  E-value: 8.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   194 MGPGRTVVVKGEVNTNAKSFNVDLVAGRSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 273
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 564391995   274 VREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDV 313
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 24-148 2.08e-49

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: 160.45  E-value: 2.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995    24 EQLKPGSLIVIRGHVPKDSERFQVDFQHGnslkPRADVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 564391995   104 IVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 17-148 1.34e-48

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: 158.57  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995  17 PYVSTITEQLKPGSLIVIRGHVPKDSERFQVDFQHGNSlkpraDVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPF 96
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564391995  97 RKEKSFEIVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 24-148 1.03e-45

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: 151.25  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   24 EQLKPGSLIVIRGHVPKDSERFQVDFQhgNSLKPRADVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPFRKEKSFE 103
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564391995  104 IVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 194-313 8.81e-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: 148.51  E-value: 8.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   194 MGPGRTVVVKGEVNTNAKSFNVDLVAGRSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 273
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 564391995   274 VREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDV 313
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 185-310 4.25e-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: 142.00  E-value: 4.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995 185 PFEARLNASMGPGRTVVVKGEVNTNAKSFNVDLVAGrSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 264
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG-SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564391995 265 YFEMIIYCDVREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRL 310
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 194-313 1.44e-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: 137.77  E-value: 1.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995  194 MGPGRTVVVKGEVNTNAKSFNVDLVAG--RSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 271
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 564391995  272 CDVREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDV 313
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-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 ...
 24-148 2.08e-49

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: 160.45  E-value: 2.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995    24 EQLKPGSLIVIRGHVPKDSERFQVDFQHGnslkPRADVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 564391995   104 IVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 17-148 1.34e-48

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: 158.57  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995  17 PYVSTITEQLKPGSLIVIRGHVPKDSERFQVDFQHGNSlkpraDVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPF 96
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564391995  97 RKEKSFEIVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 24-148 1.03e-45

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: 151.25  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   24 EQLKPGSLIVIRGHVPKDSERFQVDFQhgNSLKPRADVAFHFNPRFKRsNCIVCNTLTNEKWGWEEITHDMPFRKEKSFE 103
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564391995  104 IVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSI 148
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 18-150 7.40e-45

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 148.92  E-value: 7.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995    18 YVSTITEQLKPGSLIVIRGHVPKDSERFQVDFQHGNSlkpraDVAFHFNPRFKrSNCIVCNTLTNEKWGWEEITHDMPFR 97
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFN-ENKIVCNSKLNGSWGSEEREGGFPFQ 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564391995    98 KEKSFEIVIMVLKNKFQVAVNGKHILLYAHRINPEKIDTLGIYGKVNIHSIGF 150
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 194-313 8.81e-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: 148.51  E-value: 8.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   194 MGPGRTVVVKGEVNTNAKSFNVDLVAGRSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 273
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 564391995   274 VREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDV 313
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 185-310 4.25e-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: 142.00  E-value: 4.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995 185 PFEARLNASMGPGRTVVVKGEVNTNAKSFNVDLVAGrSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 264
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG-SSDIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564391995 265 YFEMIIYCDVREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRL 310
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 186-314 6.72e-41

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 138.90  E-value: 6.72e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995   186 FEARLNASMGPGRTVVVKGEVNTNAKSFNVDLVAGrSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERnITCFPFSSGMY 265
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG-GDDIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 564391995   266 FEMIIYCDVREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDVR 314
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 194-313 1.44e-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: 137.77  E-value: 1.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391995  194 MGPGRTVVVKGEVNTNAKSFNVDLVAG--RSRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 271
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 564391995  272 CDVREFKVAVNGVHSLEYKHRFKdLSSIDTLAVDGDIRLLDV 313
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 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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