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Conserved domains on  [gi|24655134|ref|NP_611349|]
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uncharacterized protein Dmel_CG5335 [Drosophila melanogaster]

Protein Classification

GLECT domain-containing protein( domain architecture ID 10448426)

GLECT domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 12-140 1.70e-36

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: 127.37  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    12 PLEFGHVLEVVAKTIDGAARFHINLCTAkstVDPNADIGLRFSCYFRNDVIVRNSRINGAWGEEEshvmdpNTLPNPIVS 91
Cdd:pfam00337   3 GLQPGSSLTIKGIVLPDAQRFSINLQTG---VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEE------REGGFPFQP 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 24655134    92 GEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:pfam00337  74 GQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTS 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 172-297 1.39e-27

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: 104.25  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134 172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREeLHFSVRFDEKAVVRNSMNKNfEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:cd00070  10 LKPGSTLTVKGRVLPNAK-RFSINLGTGSSDIA-LHFNPRFDENVIVRNSFLNG-NWGPEERSGGFPFQPGQPFELTILV 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24655134 252 TEREVLTAVDGYNFFSYTWRTPNAMMNLVgfkvtSINGLvVQITGV 297
Cdd:cd00070  87 EEDKFQIFVNGQHFFSFPHRLPLESIDYL-----SINGD-VSLTSV 126
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 12-140 1.70e-36

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: 127.37  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    12 PLEFGHVLEVVAKTIDGAARFHINLCTAkstVDPNADIGLRFSCYFRNDVIVRNSRINGAWGEEEshvmdpNTLPNPIVS 91
Cdd:pfam00337   3 GLQPGSSLTIKGIVLPDAQRFSINLQTG---VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEE------REGGFPFQP 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 24655134    92 GEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:pfam00337  74 GQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTS 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-140 1.18e-33

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: 120.05  E-value: 1.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134   5 FAGNLSHPLEFGHVLEVVAKTIDGAARFHINLCTAKStvdpnaDIGLRFSCYFRNDVIVRNSRINGAWGEEESHvmdpnt 84
Cdd:cd00070   2 YKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS------DIALHFNPRFDENVIVRNSFLNGNWGPEERS------ 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24655134  85 LPNPIVSGEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:cd00070  70 GGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTS 125
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 10-138 2.16e-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: 116.54  E-value: 2.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134     10 SHPLEFGHVLEVVAKTIDGAARFHINLCTakstvDPNADIGLRFSCYFRNDVIVRNSRINGAWGEEESHVmdpntlPNPI 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQC-----GPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERSG------GFPF 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 24655134     90 VSGEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQV 138
Cdd:smart00908  70 QPGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 172-297 1.39e-27

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: 104.25  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134 172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREeLHFSVRFDEKAVVRNSMNKNfEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:cd00070  10 LKPGSTLTVKGRVLPNAK-RFSINLGTGSSDIA-LHFNPRFDENVIVRNSFLNG-NWGPEERSGGFPFQPGQPFELTILV 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24655134 252 TEREVLTAVDGYNFFSYTWRTPNAMMNLVgfkvtSINGLvVQITGV 297
Cdd:cd00070  87 EEDKFQIFVNGQHFFSFPHRLPLESIDYL-----SINGD-VSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 172-288 4.52e-27

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: 102.67  E-value: 4.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREELHFSVRFDEKAVVRNSMnKNFEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:smart00908   4 LSPGSSITIRGIVLPDAK-RFSINLQCGPNADIALHFNPRFDEGTIVRNSK-QNGKWGKEERSGGFPFQPGQPFELEILV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24655134    252 TEREVLTAVDGYNFFSYTWRTPNAMMNLV----GFKVTSIN 288
Cdd:smart00908  82 EEDEFKVAVNGQHFLEFPHRLPLESIDTLeisgDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 172-288 1.28e-20

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: 85.77  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134   172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREE--LHFSVRFDEKAVVRNSMnKNFEFGSEERHGGFPFVFNQQFKLAL 249
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQ-RFSINLQTGVGPSDDiaLHFNPRFDENVIVRNSR-QNGQWGQEEREGGFPFQPGQPFELTI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24655134   250 AFTEREVLTAVDGYNFFSYTWRTPNAMMNLV----GFKVTSIN 288
Cdd:pfam00337  82 LVGDDHFKIYVNGQHFTTFKHRLPPEDIDALqvrgDVKLTSVL 124
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 12-140 1.70e-36

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: 127.37  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    12 PLEFGHVLEVVAKTIDGAARFHINLCTAkstVDPNADIGLRFSCYFRNDVIVRNSRINGAWGEEEshvmdpNTLPNPIVS 91
Cdd:pfam00337   3 GLQPGSSLTIKGIVLPDAQRFSINLQTG---VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEE------REGGFPFQP 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 24655134    92 GEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:pfam00337  74 GQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTS 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-140 1.18e-33

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: 120.05  E-value: 1.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134   5 FAGNLSHPLEFGHVLEVVAKTIDGAARFHINLCTAKStvdpnaDIGLRFSCYFRNDVIVRNSRINGAWGEEESHvmdpnt 84
Cdd:cd00070   2 YKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS------DIALHFNPRFDENVIVRNSFLNGNWGPEERS------ 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24655134  85 LPNPIVSGEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:cd00070  70 GGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTS 125
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 10-138 2.16e-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: 116.54  E-value: 2.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134     10 SHPLEFGHVLEVVAKTIDGAARFHINLCTakstvDPNADIGLRFSCYFRNDVIVRNSRINGAWGEEESHVmdpntlPNPI 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQC-----GPNADIALHFNPRFDEGTIVRNSKQNGKWGKEERSG------GFPF 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 24655134     90 VSGEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQV 138
Cdd:smart00908  70 QPGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQL 118
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 172-297 1.39e-27

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: 104.25  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134 172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREeLHFSVRFDEKAVVRNSMNKNfEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:cd00070  10 LKPGSTLTVKGRVLPNAK-RFSINLGTGSSDIA-LHFNPRFDENVIVRNSFLNG-NWGPEERSGGFPFQPGQPFELTILV 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24655134 252 TEREVLTAVDGYNFFSYTWRTPNAMMNLVgfkvtSINGLvVQITGV 297
Cdd:cd00070  87 EEDKFQIFVNGQHFFSFPHRLPLESIDYL-----SINGD-VSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 172-288 4.52e-27

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: 102.67  E-value: 4.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREELHFSVRFDEKAVVRNSMnKNFEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:smart00908   4 LSPGSSITIRGIVLPDAK-RFSINLQCGPNADIALHFNPRFDEGTIVRNSK-QNGKWGKEERSGGFPFQPGQPFELEILV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24655134    252 TEREVLTAVDGYNFFSYTWRTPNAMMNLV----GFKVTSIN 288
Cdd:smart00908  82 EEDEFKVAVNGQHFLEFPHRLPLESIDTLeisgDVQLTSVQ 122
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 5-140 7.41e-21

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 86.51  E-value: 7.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134      5 FAGNLSHPLEFGHVLEVVAKTIDGAARFHINLCTakstvdPNADIGLRFSCYFRNDVIVRNSRINGAWGEEESHVmdpnt 84
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLT------GGDDIALHFNPRFNENKIVCNSKLNGSWGSEEREG----- 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24655134     85 lPNPIVSGEFFLVYILCCEDSFAISINSREFCRFRYRMPLGTIRALEIRDQIQVIK 140
Cdd:smart00276  70 -GFPFQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTS 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 172-288 1.28e-20

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: 85.77  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134   172 FSPGHVIVLTARCFENKKgQFIIKFMDSDTKREE--LHFSVRFDEKAVVRNSMnKNFEFGSEERHGGFPFVFNQQFKLAL 249
Cdd:pfam00337   4 LQPGSSLTIKGIVLPDAQ-RFSINLQTGVGPSDDiaLHFNPRFDENVIVRNSR-QNGQWGQEEREGGFPFQPGQPFELTI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24655134   250 AFTEREVLTAVDGYNFFSYTWRTPNAMMNLV----GFKVTSIN 288
Cdd:pfam00337  82 LVGDDHFKIYVNGQHFTTFKHRLPPEDIDALqvrgDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 172-297 4.27e-15

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 70.72  E-value: 4.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655134    172 FSPGHVIVLTARCFENKKGqFIIKFmDSDTKREELHFSVRFDEKAVVRNSMNKNfEFGSEERHGGFPFVFNQQFKLALAF 251
Cdd:smart00276   9 LKPGQTLTVRGIVLPDAKR-FSINL-LTGGDDIALHFNPRFNENKIVCNSKLNG-SWGSEEREGGFPFQPGQPFDLTIIV 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 24655134    252 TEREVLTAVDGYNFFSYTWRTPNAMMNLVgfkvtSINGlVVQITGV 297
Cdd:smart00276  86 QPDHFQIFVNGVHITTFPHRLPLESIDYL-----SING-DVQLTSV 125
 
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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