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Conserved domains on  [gi|528508723|ref|XP_005173761|]
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uncharacterized protein lgals4 isoform X4 [Danio rerio]

Protein Classification

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 ...
 216-340 1.50e-42

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: 152.40  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  216 PYVGPISGGLREGMALYVKGVVPNNADRFALNFKTGisdKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKG 294
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFdENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723  295 QDFEMLTAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 534-654 2.83e-41

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: 148.51  E-value: 2.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    534 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 612
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    613 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 654
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1331-1453 1.15e-39

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: 143.93  E-value: 1.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1331 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1409
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1410 TMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1470-1590 1.57e-39

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: 143.50  E-value: 1.57e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1470 PGGLREGMAMFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VTMNSFRNGAWETEESVSDNPFKKGQHFSML 1548
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1549 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1590
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 846-966 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    846 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 924
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    925 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 966
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1158-1278 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1158 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 1236
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1237 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1278
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 707-829 2.73e-39

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: 142.78  E-value: 2.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   707 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 785
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   786 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1019-1141 3.06e-39

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: 142.78  E-value: 3.06e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1019 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1097
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1098 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 395-517 3.09e-39

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: 142.78  E-value: 3.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   395 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEML 473
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   474 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1810-1932 5.82e-39

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: 142.00  E-value: 5.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1810 PYVGPISGGLREGMAVYLQGVVPPNADKFEINFktgQSGSDDIAFHFNPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 1888
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 528508723 1889 QDFEMLTVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1637-1761 7.46e-38

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: 138.92  E-value: 7.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1637 PYVGPISGGLREGMAVYLQGVVPPNADKFQINFktgQSGSDDTAFHFNPRMGQ-IVAMNSFRNGKWETQESVSNNPFKKG 1715
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDEnVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723 1716 EAFEMFTVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1983-2110 2.75e-34

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: 128.52  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1983 PYVGSISGGLREGMALYFQGVVPPNADKFEINFktgQSGSDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKG 2061
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2062 EAFEMFMVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVSMNIF 2110
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 2156-2283 9.16e-34

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: 126.98  E-value: 9.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 2156 PYLGQIPGGLREGMTLYVKGVVPSNGDRFSINFKTGStdkDDIAFHFNPRMGSK-LVMNSMKSGRWGAEEYVSENPCKKG 2234
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGS---SDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2235 DAFEFYIQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSISFL 2283
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 22-149 2.06e-32

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: 123.13  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   22 PYVSRIHGGLKAGKGVFIQGAVPAGSDGFVVNLKCGesdGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPG 100
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEErSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  101 SSFDLNIAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 216-340 1.50e-42

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: 152.40  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  216 PYVGPISGGLREGMALYVKGVVPNNADRFALNFKTGisdKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKG 294
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFdENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723  295 QDFEMLTAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 534-654 2.83e-41

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: 148.51  E-value: 2.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    534 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 612
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    613 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 654
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 528-655 2.05e-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: 146.24  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  528 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMGQK-VVMNSFRNGAWETEESVSDNPFTKG 606
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  607 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 655
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 534-655 4.16e-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: 145.09  E-value: 4.16e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   534 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFNPRM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 612
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723   613 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 655
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1331-1453 1.15e-39

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: 143.93  E-value: 1.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1331 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1409
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1410 TMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 222-340 1.51e-39

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: 143.50  E-value: 1.51e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    222 SGGLREGMALYVKGVVPNNADRFALNFKTGISDkdDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKGQDFEML 300
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFdEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 528508723    301 TAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1470-1590 1.57e-39

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: 143.50  E-value: 1.57e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1470 PGGLREGMAMFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VTMNSFRNGAWETEESVSDNPFKKGQHFSML 1548
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1549 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1590
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 846-966 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    846 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 924
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    925 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 966
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1158-1278 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1158 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 1236
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1237 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1278
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 707-829 2.73e-39

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: 142.78  E-value: 2.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   707 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 785
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   786 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1470-1591 2.81e-39

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: 142.78  E-value: 2.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1470 PGGLREGMAMFMQGVVPDNADQFEINFKTGQSGSDDIAFHFNPRM-GQKVTMNSFRNGAWETEESVSDNPFKKGQHFSML 1548
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723  1549 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1591
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1019-1141 3.06e-39

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: 142.78  E-value: 3.06e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1019 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1097
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1098 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 395-517 3.09e-39

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: 142.78  E-value: 3.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   395 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEML 473
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   474 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1464-1591 5.39e-39

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: 142.00  E-value: 5.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1464 PYVDQIPGGLREGMAMFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMGQK-VTMNSFRNGAWETEESVSDNPFKKG 1542
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 1543 QHFSMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1591
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1810-1932 5.82e-39

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: 142.00  E-value: 5.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1810 PYVGPISGGLREGMAVYLQGVVPPNADKFEINFktgQSGSDDIAFHFNPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 1888
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 528508723 1889 QDFEMLTVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1816-1932 1.36e-38

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: 140.80  E-value: 1.36e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1816 SGGLREGMAVYLQGVVPPNADKFEINFKTGQSgsDDIAFHFNPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQDFEML 1894
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 528508723   1895 TVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDV 116
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1158-1279 2.21e-38

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: 140.08  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1158 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFKPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 1236
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723  1237 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1279
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 846-967 2.21e-38

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: 140.08  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   846 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFKPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 924
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723   925 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 967
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1152-1279 2.45e-38

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: 140.08  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1152 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 1230
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 1231 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1279
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 840-967 2.45e-38

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: 140.08  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  840 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 918
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  919 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 967
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 395-517 3.60e-38

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: 139.65  E-value: 3.60e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    395 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEML 473
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723    474 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1331-1453 4.72e-38

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: 139.26  E-value: 4.72e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1331 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1409
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   1410 TMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1816-1934 5.25e-38

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: 139.31  E-value: 5.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1816 SGGLREGMAVYLQGVVPPNADKFEINFKTGQSGSDDIAFHFNPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQDFEML 1894
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  1895 TVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGVAV 1934
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 707-829 6.82e-38

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: 138.88  E-value: 6.82e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    707 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 785
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723    786 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1637-1761 7.46e-38

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: 138.92  E-value: 7.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1637 PYVGPISGGLREGMAVYLQGVVPPNADKFQINFktgQSGSDDTAFHFNPRMGQ-IVAMNSFRNGKWETQESVSNNPFKKG 1715
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDEnVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723 1716 EAFEMFTVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 222-340 1.15e-37

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: 138.16  E-value: 1.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   222 SGGLREGMALYVKGVVPNNADRFALNFKTGISDKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKGQDFEML 300
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723   301 TAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 389-517 1.35e-37

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: 138.15  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  389 PRVVQIPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKG 467
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528508723  468 EPFEMLTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1019-1141 1.85e-37

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: 137.34  E-value: 1.85e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1019 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1097
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   1098 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1013-1141 2.27e-37

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: 137.38  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1013 PRVVQIPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKG 1091
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528508723 1092 EPFEMLTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1643-1761 3.51e-37

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: 136.57  E-value: 3.51e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1643 SGGLREGMAVYLQGVVPPNADKFQINFKTGQSgsDDTAFHFNPRMG-QIVAMNSFRNGKWETQESVSNNPFKKGEAFEMF 1721
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDeGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 528508723   1722 TVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 706-829 3.80e-37

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: 137.00  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  706 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 784
Cdd:cd00070     6 LPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPGQPFEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528508723  785 LTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:cd00070    83 TILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1330-1453 5.94e-37

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: 5.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1330 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 1408
Cdd:cd00070     6 LPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPGQPFEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528508723 1409 LTMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:cd00070    83 TILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1643-1761 8.49e-37

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: 135.85  E-value: 8.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1643 SGGLREGMAVYLQGVVPPNADKFQINFKTGQSGSDDTAFHFNPRM-GQIVAMNSFRNGKWETQESVSNNPFKKGEAFEMF 1721
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  1722 TVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1983-2110 2.75e-34

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: 128.52  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1983 PYVGSISGGLREGMALYFQGVVPPNADKFEINFktgQSGSDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKG 2061
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2062 EAFEMFMVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVSMNIF 2110
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 2156-2283 9.16e-34

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: 126.98  E-value: 9.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 2156 PYLGQIPGGLREGMTLYVKGVVPSNGDRFSINFKTGStdkDDIAFHFNPRMGSK-LVMNSMKSGRWGAEEYVSENPCKKG 2234
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGS---SDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2235 DAFEFYIQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSISFL 2283
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 2162-2281 1.19e-33

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: 126.55  E-value: 1.19e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   2162 PGGLREGMTLYVKGVVPSNGDRFSINFKTGSTDkdDIAFHFNPRMG-SKLVMNSMKSGRWGAEEYVSENPCKKGDAFEFY 2240
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFDeGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 528508723   2241 IQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSIS 2281
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLT 119
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 2162-2281 1.55e-33

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: 126.22  E-value: 1.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  2162 PGGLREGMTLYVKGVVPSNGDRFSINFKTGSTDKDDIAFHFNPRM-GSKLVMNSMKSGRWGAEEYVSENPCKKGDAFEFY 2240
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 528508723  2241 IQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSIS 2281
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLT 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1989-2106 1.22e-32

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: 123.86  E-value: 1.22e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1989 SGGLREGMALYFQGVVPPNADKFEINFKTGQSgsDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKGEAFEMF 2067
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 528508723   2068 MVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVS 2106
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQ 117
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 22-149 2.06e-32

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: 123.13  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   22 PYVSRIHGGLKAGKGVFIQGAVPAGSDGFVVNLKCGesdGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPG 100
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEErSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  101 SSFDLNIAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 28-149 3.91e-32

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: 122.31  E-value: 3.91e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723     28 HGGLKAGKGVFIQGAVPAGSDGFVVNLKCGESDgdDIAFQMKPQFISNFTAVNSRQNGSWGKEEKLD-FPLKPGSSFDLN 106
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFDEGTIVRNSKQNGKWGKEERSGgFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 528508723    107 IAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1989-2107 3.57e-31

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: 119.67  E-value: 3.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1989 SGGLREGMALYFQGVVPPNADKFEINFKTGQSGSDDIAFHFNPLMGQNL-DMNSFRNGAWETQESVSNNPFKKGEAFEMF 2067
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENViVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  2068 MVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVSM 2107
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 29-149 7.61e-31

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: 118.51  E-value: 7.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    29 GGLKAGKGVFIQGAVPAGSDGFVVNLKCGESDGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPGSSFDLNI 107
Cdd:pfam00337    2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEErEGGFPFQPGQPFELTI 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 528508723   108 AVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:pfam00337   82 LVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 216-340 1.50e-42

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: 152.40  E-value: 1.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  216 PYVGPISGGLREGMALYVKGVVPNNADRFALNFKTGisdKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKG 294
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFdENVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723  295 QDFEMLTAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 534-654 2.83e-41

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: 148.51  E-value: 2.83e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    534 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 612
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    613 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 654
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 528-655 2.05e-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: 146.24  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  528 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMGQK-VVMNSFRNGAWETEESVSDNPFTKG 606
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  607 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 655
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 534-655 4.16e-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: 145.09  E-value: 4.16e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   534 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFNPRM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 612
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723   613 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 655
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1331-1453 1.15e-39

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: 143.93  E-value: 1.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1331 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1409
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1410 TMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 222-340 1.51e-39

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: 143.50  E-value: 1.51e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    222 SGGLREGMALYVKGVVPNNADRFALNFKTGISDkdDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKGQDFEML 300
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFdEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 528508723    301 TAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1470-1590 1.57e-39

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: 143.50  E-value: 1.57e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1470 PGGLREGMAMFMQGVVPDNADQFEINFKTGQSgsDDIAFHFNPRMGQK-VTMNSFRNGAWETEESVSDNPFKKGQHFSML 1548
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1549 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1590
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 846-966 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    846 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 924
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723    925 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 966
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1158-1278 1.92e-39

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: 143.12  E-value: 1.92e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1158 PGGLREGMALFMQGVVPDNADQFEINFKTGQSgsDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQHFKML 1236
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 528508723   1237 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINS 1278
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTS 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 707-829 2.73e-39

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: 142.78  E-value: 2.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   707 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 785
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   786 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1470-1591 2.81e-39

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: 142.78  E-value: 2.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1470 PGGLREGMAMFMQGVVPDNADQFEINFKTGQSGSDDIAFHFNPRM-GQKVTMNSFRNGAWETEESVSDNPFKKGQHFSML 1548
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723  1549 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1591
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1019-1141 3.06e-39

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: 142.78  E-value: 3.06e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1019 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1097
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723  1098 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 395-517 3.09e-39

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: 142.78  E-value: 3.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   395 PGGLKEGMILYMKGAVPANADRFEINFKTGQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEML 473
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENvIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 528508723   474 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1464-1591 5.39e-39

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: 142.00  E-value: 5.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1464 PYVDQIPGGLREGMAMFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMGQK-VTMNSFRNGAWETEESVSDNPFKKG 1542
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 1543 QHFSMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1591
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1810-1932 5.82e-39

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: 142.00  E-value: 5.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1810 PYVGPISGGLREGMAVYLQGVVPPNADKFEINFktgQSGSDDIAFHFNPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 1888
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 528508723 1889 QDFEMLTVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1816-1932 1.36e-38

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: 140.80  E-value: 1.36e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1816 SGGLREGMAVYLQGVVPPNADKFEINFKTGQSgsDDIAFHFNPQMGQK-VVMNSFRNGAWETEESVSDNPFTKGQDFEML 1894
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 528508723   1895 TVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDV 116
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1158-1279 2.21e-38

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: 140.08  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1158 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFKPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 1236
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723  1237 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1279
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 846-967 2.21e-38

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: 140.08  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   846 PGGLREGMALFMQGVVPDNADQFEINFKTGQSGSDDIAFHFKPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQHFKML 924
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 528508723   925 TAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 967
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1152-1279 2.45e-38

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: 140.08  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1152 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 1230
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 1231 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1279
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 840-967 2.45e-38

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: 140.08  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  840 PYVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMGQK-VVMNSFRNGAWETEESVSDNPFTKG 918
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  919 QHFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 967
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 395-517 3.60e-38

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: 139.65  E-value: 3.60e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    395 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEML 473
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723    474 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1331-1453 4.72e-38

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: 139.26  E-value: 4.72e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1331 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1409
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   1410 TMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1816-1934 5.25e-38

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: 139.31  E-value: 5.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1816 SGGLREGMAVYLQGVVPPNADKFEINFKTGQSGSDDIAFHFNPQM-GQKVVMNSFRNGAWETEESVSDNPFTKGQDFEML 1894
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  1895 TVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGVAV 1934
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 707-829 6.82e-38

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: 138.88  E-value: 6.82e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    707 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 785
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723    786 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1637-1761 7.46e-38

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: 138.92  E-value: 7.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1637 PYVGPISGGLREGMAVYLQGVVPPNADKFQINFktgQSGSDDTAFHFNPRMGQ-IVAMNSFRNGKWETQESVSNNPFKKG 1715
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDEnVIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528508723 1716 EAFEMFTVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSL 123
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 222-340 1.15e-37

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: 138.16  E-value: 1.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   222 SGGLREGMALYVKGVVPNNADRFALNFKTGISDKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKGQDFEML 300
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723   301 TAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTL 340
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 389-517 1.35e-37

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: 138.15  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  389 PRVVQIPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKG 467
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528508723  468 EPFEMLTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 517
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1019-1141 1.85e-37

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: 137.34  E-value: 1.85e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1019 PGGLKEGMILYMKGAVPANADRFEINFKTGQsgDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEML 1097
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGP--NADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   1098 TIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1013-1141 2.27e-37

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: 137.38  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1013 PRVVQIPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKG 1091
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528508723 1092 EPFEMLTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLE 1141
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1643-1761 3.51e-37

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: 136.57  E-value: 3.51e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1643 SGGLREGMAVYLQGVVPPNADKFQINFKTGQSgsDDTAFHFNPRMG-QIVAMNSFRNGKWETQESVSNNPFKKGEAFEMF 1721
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDeGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 528508723   1722 TVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 706-829 3.80e-37

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: 137.00  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  706 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 784
Cdd:cd00070     6 LPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPGQPFEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528508723  785 LTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 829
Cdd:cd00070    83 TILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1330-1453 5.94e-37

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: 5.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1330 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 1408
Cdd:cd00070     6 LPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPGQPFEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528508723 1409 LTMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLE 1453
Cdd:cd00070    83 TILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1643-1761 8.49e-37

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: 135.85  E-value: 8.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1643 SGGLREGMAVYLQGVVPPNADKFQINFKTGQSGSDDTAFHFNPRM-GQIVAMNSFRNGKWETQESVSNNPFKKGEAFEMF 1721
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  1722 TVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSV 1761
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 217-345 2.56e-36

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 134.66  E-value: 2.56e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    217 YVGPISGGLREGMALYVKGVVPNNADRFALNFktgISDKDDVAFHFNPRM-EQKVTMNSFQNGAWGTEESVSDNPFKKGQ 295
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFnENKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 528508723    296 DFEMLTAITSAGYQVYVNGKELYTFKHHIPLEKVAVLNIGGDVTLNLFGF 345
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 706-831 1.22e-35

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 132.74  E-value: 1.22e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    706 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 784
Cdd:smart00276    5 IPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNENkIVCNSKLNGSWGSEEREGGFPFQPGQPFDL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 528508723    785 LTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLEIS 831
Cdd:smart00276   82 TIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1018-1143 1.91e-35

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 131.97  E-value: 1.91e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1018 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 1096
Cdd:smart00276    5 IPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNENkIVCNSKLNGSWGSEEREGGFPFQPGQPFDL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 528508723   1097 LTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNIGGDVAVNNLEIS 1143
Cdd:smart00276   82 TIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 394-519 2.34e-35

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 131.58  E-value: 2.34e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    394 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRMDKN-VAMNSIINGQSGTEEIISDNPFKKGEPFEM 472
Cdd:smart00276    5 IPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNENkIVCNSKLNGSWGSEEREGGFPFQPGQPFDL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 528508723    473 LTIIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLEIS 519
Cdd:smart00276   82 TIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1330-1455 2.53e-35

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 131.58  E-value: 2.53e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1330 IPGGLKEGMILYMKGAVPANADRFEINFktgQSGDDDTAFHFNPRLDKN-VAMNSVINGQSGTEEIISDNPFKKGEPFEM 1408
Cdd:smart00276    5 IPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNENkIVCNSKLNGSWGSEEREGGFPFQPGQPFDL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 528508723   1409 LTMIKPEGYQVQVNGKEQCIFKHRTPLERVSALNISGDVAVNNLEIS 1455
Cdd:smart00276   82 TIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 529-655 1.37e-34

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 129.66  E-value: 1.37e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    529 YVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMG-QKVVMNSFRNGAWETEESVSDNPFTKGQ 607
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 528508723    608 HFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 655
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSV 125
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1983-2110 2.75e-34

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: 128.52  E-value: 2.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 1983 PYVGSISGGLREGMALYFQGVVPPNADKFEINFktgQSGSDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKG 2061
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL---GTGSSDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2062 EAFEMFMVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVSMNIF 2110
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1811-1932 3.67e-34

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 128.50  E-value: 3.67e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1811 YVGPISGGLREGMAVYLQGVVPPNADKFEINFktgQSGSDDIAFHFNPQMG-QKVVMNSFRNGAWETEESVSDNPFTKGQ 1889
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 528508723   1890 DFEMLTVLQPEGYQVYVNGKVLHTFKHRMQLEKVSTLNIFGGV 1932
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDV 120
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 2156-2283 9.16e-34

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: 126.98  E-value: 9.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723 2156 PYLGQIPGGLREGMTLYVKGVVPSNGDRFSINFKTGStdkDDIAFHFNPRMGSK-LVMNSMKSGRWGAEEYVSENPCKKG 2234
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGS---SDIALHFNPRFDENvIVRNSFLNGNWGPEERSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723 2235 DAFEFYIQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSISFL 2283
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 2162-2281 1.19e-33

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: 126.55  E-value: 1.19e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   2162 PGGLREGMTLYVKGVVPSNGDRFSINFKTGSTDkdDIAFHFNPRMG-SKLVMNSMKSGRWGAEEYVSENPCKKGDAFEFY 2240
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFDeGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 528508723   2241 IQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSIS 2281
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLT 119
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 2162-2281 1.55e-33

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: 126.22  E-value: 1.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  2162 PGGLREGMTLYVKGVVPSNGDRFSINFKTGSTDKDDIAFHFNPRM-GSKLVMNSMKSGRWGAEEYVSENPCKKGDAFEFY 2240
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFdENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 528508723  2241 IQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSIS 2281
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLT 121
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1469-1591 1.78e-33

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 126.19  E-value: 1.78e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1469 IPGGLREGMAMFMQGVVPDNADQFEINFktgQSGSDDIAFHFNPRMG-QKVTMNSFRNGAWETEESVSDNPFKKGQHFSM 1547
Cdd:smart00276    5 IPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQPFDL 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   1548 LTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1591
Cdd:smart00276   82 TIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSV 125
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 841-967 4.27e-33

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 125.42  E-value: 4.27e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    841 YVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMG-QKVVMNSFRNGAWETEESVSDNPFTKGQ 919
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 528508723    920 HFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 967
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSV 125
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1153-1279 4.27e-33

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 125.42  E-value: 4.27e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1153 YVGQVPGGLREGMALFMQGVVPDNADQFEINFktgQSGSDDIAFHFKPQMG-QKVVMNSFRNGAWETEESVSDNPFTKGQ 1231
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 528508723   1232 HFKMLTAITSAGYQVYVNDKELCTFKHRLPLERLSTLNISGNVAINSL 1279
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSV 125
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1989-2106 1.22e-32

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: 123.86  E-value: 1.22e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1989 SGGLREGMALYFQGVVPPNADKFEINFKTGQSgsDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKGEAFEMF 2067
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPN--ADIALHFNPRFDEGtIVRNSKQNGKWGKEERSGGFPFQPGQPFELE 78

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 528508723   2068 MVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVS 2106
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQ 117
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 22-149 2.06e-32

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: 123.13  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   22 PYVSRIHGGLKAGKGVFIQGAVPAGSDGFVVNLKCGesdGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPG 100
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTG---SSDIALHFNPRFDENVIVRNSFLNGNWGPEErSGGFPFQPG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528508723  101 SSFDLNIAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:cd00070    78 QPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1638-1762 3.31e-32

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 122.72  E-value: 3.31e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1638 YVGPISGGLREGMAVYLQGVVPPNADKFQINFktgQSGSDDTAFHFNPRMG-QIVAMNSFRNGKWETQESVSNNPFKKGE 1716
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNeNKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 528508723   1717 AFEMFTVIKSEGYQVYVNGKEHYTFKHRIPLEKVSTLSIVGGVSVK 1762
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLT 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 28-149 3.91e-32

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: 122.31  E-value: 3.91e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723     28 HGGLKAGKGVFIQGAVPAGSDGFVVNLKCGESDgdDIAFQMKPQFISNFTAVNSRQNGSWGKEEKLD-FPLKPGSSFDLN 106
Cdd:smart00908    1 PGGLSPGSSITIRGIVLPDAKRFSINLQCGPNA--DIALHFNPRFDEGTIVRNSKQNGKWGKEERSGgFPFQPGQPFELE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 528508723    107 IAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:smart00908   79 ILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1989-2107 3.57e-31

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: 119.67  E-value: 3.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723  1989 SGGLREGMALYFQGVVPPNADKFEINFKTGQSGSDDIAFHFNPLMGQNL-DMNSFRNGAWETQESVSNNPFKKGEAFEMF 2067
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENViVRNSRQNGQWGQEEREGGFPFQPGQPFELT 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 528508723  2068 MVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVSM 2107
Cdd:pfam00337   81 ILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKL 120
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 29-149 7.61e-31

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: 118.51  E-value: 7.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723    29 GGLKAGKGVFIQGAVPAGSDGFVVNLKCGESDGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPGSSFDLNI 107
Cdd:pfam00337    2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGVGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEErEGGFPFQPGQPFELTI 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 528508723   108 AVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNV 149
Cdd:pfam00337   82 LVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 23-152 3.38e-30

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 116.94  E-value: 3.38e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723     23 YVSRIHGGLKAGKGVFIQGAVPAGSDGFVVNLKCGesdGDDIAFQMKPQFISNFTAVNSRQNGSWGKEE-KLDFPLKPGS 101
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTG---GDDIALHFNPRFNENKIVCNSKLNGSWGSEErEGGFPFQPGQ 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 528508723    102 SFDLNIAVNSEGYQVFLSGQEVGCFQHRISLERVNTLAVAGGVSLTNVMFT 152
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSFE 128
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 2157-2285 1.24e-29

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 115.40  E-value: 1.24e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   2157 YLGQIPGGLREGMTLYVKGVVPSNGDRFSINFKTGStdkDDIAFHFNPRMGS-KLVMNSMKSGRWGAEEYVSENPCKKGD 2235
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGG---DDIALHFNPRFNEnKIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 528508723   2236 AFEFYIQIKAEGYQVQFKDHKQSMFKHRIPFERVTTINVLGNVSISFLGF 2285
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 1984-2106 5.05e-29

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 113.48  E-value: 5.05e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528508723   1984 YVGSISGGLREGMALYFQGVVPPNADKFEINFktgQSGSDDIAFHFNPLMGQN-LDMNSFRNGAWETQESVSNNPFKKGE 2062
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL---LTGGDDIALHFNPRFNENkIVCNSKLNGSWGSEEREGGFPFQPGQ 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 528508723   2063 AFEMFMVIKSEGYQVYVNENDLYTFKHRIPLEKVSILNIVGAVS 2106
Cdd:smart00276   78 PFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQ 121
 
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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