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Conserved domains on  [gi|291223180|ref|XP_002731585|]
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PREDICTED: galectin-8-like [Saccoglossus kowalevskii]

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 ...
 214-339 6.70e-54

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: 172.78  E-value: 6.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   214 PNGMFPGRMVIINGTVAPNPTRFMVNFQIGHSqgkaHDVVFHFNPRFPANVIVRNSRQQQKWGPEERTaPYFPFQANTNF 293
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN----ADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 291223180   294 EIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 54-180 1.06e-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: 159.68  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180    54 PGCMRPGTMVVIQGSVPPNADRFAINFQIGastkPRADIAFHFAARVKAGHIVRNTLTNEKWGAEERGvPYQPFVPGQNF 133
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 291223180   134 EIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSV 121
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 214-339 6.70e-54

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: 172.78  E-value: 6.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   214 PNGMFPGRMVIINGTVAPNPTRFMVNFQIGHSqgkaHDVVFHFNPRFPANVIVRNSRQQQKWGPEERTaPYFPFQANTNF 293
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN----ADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 291223180   294 EIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 208-339 4.34e-50

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: 163.19  E-value: 4.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180 208 PYVGAIPNGMFPGRMVIINGTVAPNPTRFMVNFQighsqGKAHDVVFHFNPRFPANVIVRNSRQQQKWGPEERtAPYFPF 287
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLG-----TGSSDIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 291223180 288 QANTNFEIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 54-180 1.06e-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: 159.68  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180    54 PGCMRPGTMVVIQGSVPPNADRFAINFQIGastkPRADIAFHFAARVKAGHIVRNTLTNEKWGAEERGvPYQPFVPGQNF 133
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 291223180   134 EIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 214-339 4.83e-48

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: 157.80  E-value: 4.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180  214 PNGMFPGRMVIINGTVAPNPTRFMVNFQIGhsQGKAHDVVFHFNPRFPANVIVRNSRQQQKWGPEERTaPYFPFQANTNF 293
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 291223180  294 EIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 54-180 3.78e-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: 150.48  E-value: 3.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   54 PGCMRPGTMVVIQGSVPPNADRFAINFQigASTKPRADIAFHFAARVKAGHIVRNTLTNEKWGAEERGvPYQPFVPGQNF 133
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 291223180  134 EIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRL-PPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 48-180 1.99e-44

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: 148.55  E-value: 1.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180  48 PFLGQIPGCMRPGTMVVIQGSVPPNADRFAINFQIGAStkpraDIAFHFAARVKAGHIVRNTLTNEKWGAEERgVPYQPF 127
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 291223180 128 VPGQNFEIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRL-PLESIDYLSINGDVSLTSV 126
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 214-339 6.70e-54

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: 172.78  E-value: 6.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   214 PNGMFPGRMVIINGTVAPNPTRFMVNFQIGHSqgkaHDVVFHFNPRFPANVIVRNSRQQQKWGPEERTaPYFPFQANTNF 293
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN----ADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 291223180   294 EIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 208-339 4.34e-50

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: 163.19  E-value: 4.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180 208 PYVGAIPNGMFPGRMVIINGTVAPNPTRFMVNFQighsqGKAHDVVFHFNPRFPANVIVRNSRQQQKWGPEERtAPYFPF 287
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLG-----TGSSDIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 291223180 288 QANTNFEIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 54-180 1.06e-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: 159.68  E-value: 1.06e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180    54 PGCMRPGTMVVIQGSVPPNADRFAINFQIGastkPRADIAFHFAARVKAGHIVRNTLTNEKWGAEERGvPYQPFVPGQNF 133
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 291223180   134 EIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 214-339 4.83e-48

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: 157.80  E-value: 4.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180  214 PNGMFPGRMVIINGTVAPNPTRFMVNFQIGhsQGKAHDVVFHFNPRFPANVIVRNSRQQQKWGPEERTaPYFPFQANTNF 293
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 291223180  294 EIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQI 339
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 54-180 3.78e-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: 150.48  E-value: 3.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   54 PGCMRPGTMVVIQGSVPPNADRFAINFQigASTKPRADIAFHFAARVKAGHIVRNTLTNEKWGAEERGvPYQPFVPGQNF 133
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQ--TGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 291223180  134 EIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRL-PPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 48-180 1.99e-44

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: 148.55  E-value: 1.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180  48 PFLGQIPGCMRPGTMVVIQGSVPPNADRFAINFQIGAStkpraDIAFHFAARVKAGHIVRNTLTNEKWGAEERgVPYQPF 127
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDENVIVRNSFLNGNWGPEER-SGGFPF 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 291223180 128 VPGQNFEIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSV 180
Cdd:cd00070   75 QPGQPFELTILVEEDKFQIFVNGQHFFSFPHRL-PLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 209-341 3.93e-43

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 145.45  E-value: 3.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180   209 YVGAIPNGMFPGRMVIINGTVAPNPTRFMVNFQighsQGKAhDVVFHFNPRFPANVIVRNSRQQQKWGPEERTAPyFPFQ 288
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLL----TGGD-DIALHFNPRFNENKIVCNSKLNGSWGSEEREGG-FPFQ 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 291223180   289 ANTNFEIIILCQNDCYKVAVNGSHLLEYRHRIAYQQVDTLHVGGDVRINQIRY 341
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 49-182 2.22e-39

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 135.43  E-value: 2.22e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291223180    49 FLGQIPGCMRPGTMVVIQGSVPPNADRFAINFQIGAStkpraDIAFHFAARVKAGHIVRNTLTNEKWGAEERgVPYQPFV 128
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFNENKIVCNSKLNGSWGSEER-EGGFPFQ 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 291223180   129 PGQNFEIMVLAVKEEFKVAVNGQHYITYKHRVrPLKKIDYLAINGDVTITSVRF 182
Cdd:smart00276  75 PGQPFDLTIIVQPDHFQIFVNGVHITTFPHRL-PLESIDYLSINGDVQLTSVSF 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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