NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755544289|ref|XP_011242622|]
View 

galectin-8 isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.18e-47

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: 156.21  E-value: 1.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289    24 EQLKPGSLIVIRGHVPKDSERFQVDFQLGnslkPRADVAFHFNPRFKRSsCIVCNTLTQEKWGWEEITYDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755544289   104 IVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
203-322 2.85e-44

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: 147.74  E-value: 2.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   203 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 282
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 755544289   283 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 322
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 1.18e-47

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: 156.21  E-value: 1.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289    24 EQLKPGSLIVIRGHVPKDSERFQVDFQLGnslkPRADVAFHFNPRFKRSsCIVCNTLTQEKWGWEEITYDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755544289   104 IVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
17-148 3.31e-46

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: 152.79  E-value: 3.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289  17 PYVGTITEQLKPGSLIVIRGHVPKDSERFQVDFQLGNSlkpraDVAFHFNPRFKRSsCIVCNTLTQEKWGWEEITYDMPF 96
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPF 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544289  97 RKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
24-148 2.75e-44

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: 147.79  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   24 EQLKPGSLIVIRGHVPKDSERFQVDFQlgNSLKPRADVAFHFNPRFKRSScIVCNTLTQEKWGWEEITYDMPFRKEKSFE 103
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDENV-IVRNSRQNGQWGQEEREGGFPFQPGQPFE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755544289  104 IVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
203-322 2.85e-44

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: 147.74  E-value: 2.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   203 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 282
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 755544289   283 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 322
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
194-319 1.55e-41

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: 140.85  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289 194 PFEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKTrDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 273
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755544289 274 YFEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRL 319
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
203-322 2.54e-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: 137.39  E-value: 2.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289  203 MGPGRTVVIKGEVNTNARSFNVDLVAG--KTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 280
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755544289  281 CDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 322
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 1.18e-47

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: 156.21  E-value: 1.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289    24 EQLKPGSLIVIRGHVPKDSERFQVDFQLGnslkPRADVAFHFNPRFKRSsCIVCNTLTQEKWGWEEITYDMPFRKEKSFE 103
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755544289   104 IVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
17-148 3.31e-46

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: 152.79  E-value: 3.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289  17 PYVGTITEQLKPGSLIVIRGHVPKDSERFQVDFQLGNSlkpraDVAFHFNPRFKRSsCIVCNTLTQEKWGWEEITYDMPF 96
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDEN-VIVRNSFLNGNWGPEERSGGFPF 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755544289  97 RKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
24-148 2.75e-44

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: 147.79  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   24 EQLKPGSLIVIRGHVPKDSERFQVDFQlgNSLKPRADVAFHFNPRFKRSScIVCNTLTQEKWGWEEITYDMPFRKEKSFE 103
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDENV-IVRNSRQNGQWGQEEREGGFPFQPGQPFE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755544289  104 IVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSI 148
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
203-322 2.85e-44

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: 147.74  E-value: 2.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   203 MGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNiTCFPFSSGMYFEMIIYCD 282
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 755544289   283 VREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 322
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
194-319 1.55e-41

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: 140.85  E-value: 1.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289 194 PFEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKTrDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGM 273
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERSGG-FPFQPGQ 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755544289 274 YFEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRL 319
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
203-322 2.54e-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: 137.39  E-value: 2.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289  203 MGPGRTVVIKGEVNTNARSFNVDLVAG--KTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITcFPFSSGMYFEMIIY 280
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGG-FPFQPGQPFELTIL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755544289  281 CDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDV 322
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
195-323 2.80e-40

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 137.36  E-value: 2.80e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289   195 FEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKtRDIALHLNPRLNVKAFVRNSFLQDAWGEEERnITCFPFSSGMY 274
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGG-DDIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQPGQP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 755544289   275 FEMIIYCDVREFKVAINGVHSLEYKHRFKdLSSIDTLSVDGDIRLLDVR 323
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
18-150 2.14e-39

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 135.05  E-value: 2.14e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544289    18 YVGTITEQLKPGSLIVIRGHVPKDSERFQVDFQLGNSlkpraDVAFHFNPRFKrSSCIVCNTLTQEKWGWEEITYDMPFR 97
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFN-ENKIVCNSKLNGSWGSEEREGGFPFQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755544289    98 KEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSIGF 150
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH