NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|45360627|ref|NP_988986|]
View 

galectin-3 [Xenopus tropicalis]

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 ...
 129-252 1.51e-46

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: 151.20  E-value: 1.51e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    129 PSGVVHRLVITIHGTVNPNAKRFAIDFRRGH--DIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQPFKL 206
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPnaDIALHFNPRFDE--GTIVRNSKQNGKWGKEERSG-GFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 45360627    207 QVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 61-136 6.41e-06

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    61 QQYPG---------PFPGQQYPGFPPPGQGYPgfPAPGQGNPGFPAQdpQKPGAPGQPEYPAPSALVQLKVPYELPLPSG 131
Cdd:TIGR01628 407 QQFNGqplgwprmsMMPTPMGPGGPLRPNGLA--PMNAVRAPSRNAQ--NAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482


                  ....*
gi 45360627   132 VVHRL 136
Cdd:TIGR01628 483 TASQG 487
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 129-252 1.51e-46

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: 151.20  E-value: 1.51e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    129 PSGVVHRLVITIHGTVNPNAKRFAIDFRRGH--DIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQPFKL 206
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPnaDIALHFNPRFDE--GTIVRNSKQNGKWGKEERSG-GFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 45360627    207 QVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 123-252 5.66e-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: 150.09  E-value: 5.66e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627 123 PYELPLPSGVVHRLVITIHGTVNPNAKRFAIDFRRG-HDIAMHINPRFDErpHVIVRNSMIHNKWGHEERHaQKFPFVAG 201
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDE--NVIVRNSFLNGNWGPEERS-GGFPFQPG 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 45360627 202 QPFKLQVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 137-251 1.49e-35

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: 123.13  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627   137 VITIHGTVNPNAKRFAIDFRRGH----DIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQPFKLQVMCEA 212
Cdd:pfam00337   9 SLTIKGIVLPDAQRFSINLQTGVgpsdDIALHFNPRFDE--NVIVRNSRQNGQWGQEEREG-GFPFQPGQPFELTILVGD 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 45360627   213 DHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEV 251
Cdd:pfam00337  86 DHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 61-136 6.41e-06

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    61 QQYPG---------PFPGQQYPGFPPPGQGYPgfPAPGQGNPGFPAQdpQKPGAPGQPEYPAPSALVQLKVPYELPLPSG 131
Cdd:TIGR01628 407 QQFNGqplgwprmsMMPTPMGPGGPLRPNGLA--PMNAVRAPSRNAQ--NAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482


                  ....*
gi 45360627   132 VVHRL 136
Cdd:TIGR01628 483 TASQG 487
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 129-252 1.51e-46

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: 151.20  E-value: 1.51e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    129 PSGVVHRLVITIHGTVNPNAKRFAIDFRRGH--DIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQPFKL 206
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPnaDIALHFNPRFDE--GTIVRNSKQNGKWGKEERSG-GFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 45360627    207 QVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLP-LESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 123-252 5.66e-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: 150.09  E-value: 5.66e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627 123 PYELPLPSGVVHRLVITIHGTVNPNAKRFAIDFRRG-HDIAMHINPRFDErpHVIVRNSMIHNKWGHEERHaQKFPFVAG 201
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGsSDIALHFNPRFDE--NVIVRNSFLNGNWGPEERS-GGFPFQPG 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 45360627 202 QPFKLQVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:cd00070  78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 124-252 1.96e-41

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 138.51  E-value: 1.96e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    124 YELPLPSGVVHRLVITIHGTVNPNAKRFAIDFRRG-HDIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQ 202
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGgDDIALHFNPRFNE--NKIVCNSKLNGSWGSEEREG-GFPFQPGQ 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 45360627    203 PFKLQVMCEADHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEVT 252
Cdd:smart00276  78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLP-LESIDYLSINGDVQLTSVS 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 137-251 1.49e-35

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: 123.13  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627   137 VITIHGTVNPNAKRFAIDFRRGH----DIAMHINPRFDErpHVIVRNSMIHNKWGHEERHAqKFPFVAGQPFKLQVMCEA 212
Cdd:pfam00337   9 SLTIKGIVLPDAQRFSINLQTGVgpsdDIALHFNPRFDE--NVIVRNSRQNGQWGQEEREG-GFPFQPGQPFELTILVGD 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 45360627   213 DHYKVAINNETLFQYVHRVKeLHEIRSVCIAGDVTLNEV 251
Cdd:pfam00337  86 DHFKIYVNGQHFTTFKHRLP-PEDIDALQVRGDVKLTSV 123
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 61-136 6.41e-06

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 46.72  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45360627    61 QQYPG---------PFPGQQYPGFPPPGQGYPgfPAPGQGNPGFPAQdpQKPGAPGQPEYPAPSALVQLKVPYELPLPSG 131
Cdd:TIGR01628 407 QQFNGqplgwprmsMMPTPMGPGGPLRPNGLA--PMNAVRAPSRNAQ--NAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482


                  ....*
gi 45360627   132 VVHRL 136
Cdd:TIGR01628 483 TASQG 487
 
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