NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|558157769|ref|XP_006122134|]
View 

galectin-8 isoform X3 [Pelodiscus sinensis]

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 ...
 30-154 1.58e-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: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769    30 GGLHPGELVLIRGNVPDDSDRFQVDFQCGnstkPRADVAFHFNPRFKRsGFIVCNTLEKERWGWEEITYEMPFQKGKPFE 109
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 558157769   110 IVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTI 154
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 181-300 1.21e-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: 150.43  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   181 LRSGRTIVIKGEVNKNANSFAVNLKSSDSKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDvIHFPFSPGMYFELLLFCD 260
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 558157769   261 VHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDV 300
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 ...
 30-154 1.58e-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: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769    30 GGLHPGELVLIRGNVPDDSDRFQVDFQCGnstkPRADVAFHFNPRFKRsGFIVCNTLEKERWGWEEITYEMPFQKGKPFE 109
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 558157769   110 IVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTI 154
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 23-154 4.51e-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: 151.63  E-value: 4.51e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769  23 PYTGTILGGLHPGELVLIRGNVPDDSDRFQVDFQCGNStkpraDVAFHFNPRFKRsGFIVCNTLEKERWGWEEITYEMPF 102
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 558157769 103 QKGKPFEIVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTI 154
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 181-300 1.21e-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: 150.43  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   181 LRSGRTIVIKGEVNKNANSFAVNLKSSDSKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDvIHFPFSPGMYFELLLFCD 260
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 558157769   261 VHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDV 300
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 30-151 3.00e-43

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: 144.32  E-value: 3.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   30 GGLHPGELVLIRGNVPDDSDRFQVDFQCGnsTKPRADVAFHFNPRFKRSgFIVCNTLEKERWGWEEITYEMPFQKGKPFE 109
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 558157769  110 IVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQI 151
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 181-300 3.45e-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: 136.62  E-value: 3.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769  181 LRSGRTIVIKGEVNKNANSFAVNLKSSD--SKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDViHFPFSPGMYFELLLF 258
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGVgpSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREG-GFPFQPGQPFELTIL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 558157769  259 CDVHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDV 300
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 172-297 4.00e-40

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: 136.22  E-value: 4.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769 172 PYVARLNSALRSGRTIVIKGEVNKNANSFAVNLKSSDSkDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDvIHFPFSPGM 251
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPFQPGQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 558157769 252 YFELLLFCDVHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQL 297
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 30-154 1.58e-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: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769    30 GGLHPGELVLIRGNVPDDSDRFQVDFQCGnstkPRADVAFHFNPRFKRsGFIVCNTLEKERWGWEEITYEMPFQKGKPFE 109
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPFE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 558157769   110 IVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTI 154
Cdd:smart00908  77 LEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 23-154 4.51e-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: 151.63  E-value: 4.51e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769  23 PYTGTILGGLHPGELVLIRGNVPDDSDRFQVDFQCGNStkpraDVAFHFNPRFKRsGFIVCNTLEKERWGWEEITYEMPF 102
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 558157769 103 QKGKPFEIVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTI 154
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 181-300 1.21e-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: 150.43  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   181 LRSGRTIVIKGEVNKNANSFAVNLKSSDSKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDvIHFPFSPGMYFELLLFCD 260
Cdd:smart00908   4 LSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILVE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 558157769   261 VHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDV 300
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 30-151 3.00e-43

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: 144.32  E-value: 3.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   30 GGLHPGELVLIRGNVPDDSDRFQVDFQCGnsTKPRADVAFHFNPRFKRSgFIVCNTLEKERWGWEEITYEMPFQKGKPFE 109
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDEN-VIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 558157769  110 IVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQI 151
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 181-300 3.45e-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: 136.62  E-value: 3.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769  181 LRSGRTIVIKGEVNKNANSFAVNLKSSD--SKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDViHFPFSPGMYFELLLF 258
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQRFSINLQTGVgpSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREG-GFPFQPGQPFELTIL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 558157769  259 CDVHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDV 300
Cdd:pfam00337  83 VGDDHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 172-297 4.00e-40

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: 136.22  E-value: 4.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769 172 PYVARLNSALRSGRTIVIKGEVNKNANSFAVNLKSSDSkDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDvIHFPFSPGM 251
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPFQPGQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 558157769 252 YFELLLFCDVHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQL 297
Cdd:cd00070   79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSL 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 24-156 1.39e-39

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 135.05  E-value: 1.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769    24 YTGTILGGLHPGELVLIRGNVPDDSDRFQVDFQCGNStkpraDVAFHFNPRFKrSGFIVCNTLEKERWGWEEITYEMPFQ 103
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFN-ENKIVCNSKLNGSWGSEEREGGFPFQ 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 558157769   104 KGKPFEIVFMVLKDKFQVSVNKNHLLLYNHRVNLERIDTLGIYGKVQIQTIGF 156
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 173-301 1.36e-38

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 132.35  E-value: 1.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558157769   173 YVARLNSALRSGRTIVIKGEVNKNANSFAVNLkSSDSKDIALHLNPRIKTKVFVRNSYLYDSWGEEEKDViHFPFSPGMY 252
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL-LTGGDDIALHFNPRFNENKIVCNSKLNGSWGSEEREG-GFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 558157769   253 FELLLFCDVHHYKVAINGVHILEYKHRFKqLEKINVLEVTGDIQLLDVR 301
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
 
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