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Conserved domains on  [gi|1335152353|ref|XP_023616309|]
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galectin-4 isoform X1 [Myotis lucifugus]

Protein Classification

galectin family protein( domain architecture ID 10049222)

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
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 42-171 1.35e-55

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: 177.83  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  42 PYNKPIPGGLSVGMSIYIQGVASEHMKRFSVNFVAGQGpgaDIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRK 121
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS---DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPFQP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335152353 122 GTPFELVFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSI 171
Cdd:cd00070    77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 216-309 2.43e-31

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: 115.04  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353 216 PFMGKLQGGLTARKTIIVKGYVPPTGKRFAINFKVGSSgDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQ 295
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPFQPGQ 78

                          90
                  ....*....|....
gi 1335152353 296 YFDVSLAFFPTSLQ 309
Cdd:cd00070    79 PFELTILVEEDKFQ 92
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 42-171 1.35e-55

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: 177.83  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  42 PYNKPIPGGLSVGMSIYIQGVASEHMKRFSVNFVAGQGpgaDIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRK 121
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS---DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPFQP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335152353 122 GTPFELVFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSI 171
Cdd:cd00070    77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 48-172 1.50e-55

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: 177.78  E-value: 1.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353   48 PGGLSVGMSIYIQGVASEHMKRFSVNFvaGQGPGADIAFHFNPRFDGWdKVVFNSQQGGQWGSEEKKRSMPFRKGTPFEL 127
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINL--QCGPNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1335152353  128 VFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSIN 172
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 48-172 5.04e-53

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: 171.28  E-value: 5.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  48 PGGLSVGMSIYIQGVASEHMKRFSVNFVAGQGPGADIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRKGTPFEL 127
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1335152353 128 VFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSIN 172
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 216-309 2.43e-31

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: 115.04  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353 216 PFMGKLQGGLTARKTIIVKGYVPPTGKRFAINFKVGSSgDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQ 295
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPFQPGQ 78

                          90
                  ....*....|....
gi 1335152353 296 YFDVSLAFFPTSLQ 309
Cdd:cd00070    79 PFELTILVEEDKFQ 92
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 222-317 5.59e-30

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: 111.14  E-value: 5.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  222 QGGLTARKTIIVKGYVPPTGKRFAINFKVGSSGDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQYFDVSL 301
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEI 79

                           90
                   ....*....|....*.
gi 1335152353  302 AFFPTSLQCLCPGHSL 317
Cdd:smart00908  80 LVEEDEFKVAVNGQHF 95
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 222-309 1.07e-25

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: 100.02  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353 222 QGGLTARKTIIVKGYVPPTGKRFAINF--KVGSSGDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQYFDV 299
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLqtGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPFEL 79

                          90
                  ....*....|
gi 1335152353 300 SLAFFPTSLQ 309
Cdd:pfam00337  80 TILVGDDHFK 89
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 42-171 1.35e-55

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: 177.83  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  42 PYNKPIPGGLSVGMSIYIQGVASEHMKRFSVNFVAGQGpgaDIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRK 121
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS---DIALHFNPRFDE-NVIVRNSFLNGNWGPEERSGGFPFQP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335152353 122 GTPFELVFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSI 171
Cdd:cd00070    77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 48-172 1.50e-55

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: 177.78  E-value: 1.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353   48 PGGLSVGMSIYIQGVASEHMKRFSVNFvaGQGPGADIAFHFNPRFDGWdKVVFNSQQGGQWGSEEKKRSMPFRKGTPFEL 127
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINL--QCGPNADIALHFNPRFDEG-TIVRNSKQNGKWGKEERSGGFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1335152353  128 VFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSIN 172
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 48-172 5.04e-53

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: 171.28  E-value: 5.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  48 PGGLSVGMSIYIQGVASEHMKRFSVNFVAGQGPGADIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRKGTPFEL 127
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDE-NVIVRNSRQNGQWGQEEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1335152353 128 VFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSIN 172
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 43-173 4.34e-49

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 161.24  E-value: 4.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353   43 YNKPIPGGLSVGMSIYIQGVASEHMKRFSVNFVAGqgpGADIAFHFNPRFDGwDKVVFNSQQGGQWGSEEKKRSMPFRKG 122
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG---GDDIALHFNPRFNE-NKIVCNSKLNGSWGSEEREGGFPFQPG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1335152353  123 TPFELVFMVLPEHYKVVVNGNPFYEFGHRLPLQMVTHLQVDGDLELQSINF 173
Cdd:smart00276  77 QPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 216-309 2.43e-31

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: 115.04  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353 216 PFMGKLQGGLTARKTIIVKGYVPPTGKRFAINFKVGSSgDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQ 295
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-DIALHFNPRFDENVIVRNSFLNGNWGPEERS-GGFPFQPGQ 78

                          90
                  ....*....|....
gi 1335152353 296 YFDVSLAFFPTSLQ 309
Cdd:cd00070    79 PFELTILVEEDKFQ 92
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 222-317 5.59e-30

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: 111.14  E-value: 5.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  222 QGGLTARKTIIVKGYVPPTGKRFAINFKVGSSGDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQYFDVSL 301
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERS-GGFPFQPGQPFELEI 79

                           90
                   ....*....|....*.
gi 1335152353  302 AFFPTSLQCLCPGHSL 317
Cdd:smart00908  80 LVEEDEFKVAVNGQHF 95
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 217-309 2.69e-29

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 109.62  E-value: 2.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353  217 FMGKLQGGLTARKTIIVKGYVPPTGKRFAINFkVGSSGDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQY 296
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL-LTGGDDIALHFNPRFNENKIVCNSKLNGSWGSEERE-GGFPFQPGQP 78

                           90
                   ....*....|...
gi 1335152353  297 FDVSLAFFPTSLQ 309
Cdd:smart00276  79 FDLTIIVQPDHFQ 91
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 222-309 1.07e-25

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: 100.02  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335152353 222 QGGLTARKTIIVKGYVPPTGKRFAINF--KVGSSGDLALHINPRLVEGTVVRNSYLNGSWGSEEKKiSYNPFGCGQYFDV 299
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLqtGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEERE-GGFPFQPGQPFEL 79

                          90
                  ....*....|
gi 1335152353 300 SLAFFPTSLQ 309
Cdd:pfam00337  80 TILVGDDHFK 89
 
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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