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Conserved domains on  [gi|42544187|ref|NP_963837|]
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galectin-8 isoform b [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 ...
24-149 2.66e-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: 2.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187     24 PDQLDPGTLIVIRGHVPSDADRFQVDLQNGssmkPRADVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFKREKSF 103
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 42544187    104 EIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
194-314 8.04e-48

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: 156.60  E-value: 8.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    194 PMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNiTSFPFSPGMYFEMIIYC 273
Cdd:smart00908   3 GLSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILV 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 42544187    274 DVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:smart00908  82 EEDEFKVAVNGQHFLEFPHRLP-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 ...
24-149 2.66e-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: 2.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187     24 PDQLDPGTLIVIRGHVPSDADRFQVDLQNGssmkPRADVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFKREKSF 103
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 42544187    104 EIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
24-149 2.71e-49

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: 160.50  E-value: 2.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    24 PDQLDPGTLIVIRGHVPSDADRFQVDLQNGssMKPRADVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFKREKSF 103
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 42544187   104 EIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
194-314 8.04e-48

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: 156.60  E-value: 8.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    194 PMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNiTSFPFSPGMYFEMIIYC 273
Cdd:smart00908   3 GLSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILV 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 42544187    274 DVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:smart00908  82 EEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
18-149 9.22e-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: 156.64  E-value: 9.22e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187  18 PFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSmkpraDVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPF 97
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544187  98 KREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:cd00070  75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
186-314 1.81e-45

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: 150.48  E-value: 1.81e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187 186 PFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSkDIALHLNPRLNIKAFVRNSFLQESWGEEERnITSFPFSPGM 265
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPFQPGQ 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 42544187 266 YFEMIIYCDVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:cd00070  79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
192-314 2.42e-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: 145.09  E-value: 2.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187   192 NTPMGPGRTVVVKGEVNANAKSFNVDLLAG--KSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNiTSFPFSPGMYFEM 269
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPFEL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 42544187   270 IIYCDVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLP-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 ...
24-149 2.66e-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: 2.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187     24 PDQLDPGTLIVIRGHVPSDADRFQVDLQNGssmkPRADVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFKREKSF 103
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDE-GTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 42544187    104 EIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
24-149 2.71e-49

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: 160.50  E-value: 2.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    24 PDQLDPGTLIVIRGHVPSDADRFQVDLQNGssMKPRADVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFKREKSF 103
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 42544187   104 EIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
194-314 8.04e-48

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: 156.60  E-value: 8.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    194 PMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNiTSFPFSPGMYFEMIIYC 273
Cdd:smart00908   3 GLSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEILV 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 42544187    274 DVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:smart00908  82 EEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
18-149 9.22e-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: 156.64  E-value: 9.22e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187  18 PFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSmkpraDVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPF 97
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPF 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42544187  98 KREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSI 149
Cdd:cd00070  75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
186-314 1.81e-45

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: 150.48  E-value: 1.81e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187 186 PFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSkDIALHLNPRLNIKAFVRNSFLQESWGEEERnITSFPFSPGM 265
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPFQPGQ 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 42544187 266 YFEMIIYCDVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:cd00070  79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
187-315 3.11e-44

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 147.37  E-value: 3.11e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187    187 FAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSkDIALHLNPRLNIKAFVRNSFLQESWGEEERnITSFPFSPGMY 266
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-DIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQPGQP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 42544187    267 FEMIIYCDVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEVR 315
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
19-152 1.37e-43

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 145.83  E-value: 1.37e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187     19 FVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSmkpraDVAFHFNPRFKRaGCIVCNTLINEKWGREEITYDTPFK 98
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFNE-NKIVCNSKLNGSWGSEEREGGFPFQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 42544187     99 REKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFS 152
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
192-314 2.42e-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: 145.09  E-value: 2.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544187   192 NTPMGPGRTVVVKGEVNANAKSFNVDLLAG--KSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNiTSFPFSPGMYFEM 269
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGvgPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPFEL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 42544187   270 IIYCDVREFKVAVNGVHSLEYKHRFKeLSSIDTLEINGDIHLLEV 314
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLP-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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