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Conserved domains on  [gi|333470493|gb|EAL38639|]
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AGAP001197-PA, partial [Anopheles gambiae str. PEST]

Protein Classification

galectin family protein( domain architecture ID 10658251)

galectin family protein may exclusively bind beta-galactosides such as lactose in a manner independent of metal ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 11-143 1.52e-24

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: 91.50  E-value: 1.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493    11 PRYPENGDEVFIRGKLKDDAKSFSVNFClprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQEEVlDNY 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQ---------CGPNADIALHFNPRFDEG----TIVRNsKQNGKWGKEER-SGG 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333470493    90 WHVDRSQTFRVVFRLHEDCIKVFVNsvDHPPdYQFPVQLPLDQIESIELWDDVE 143
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVN--GQHF-LEFPHRLPLESIDTLEISGDVQ 117
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 11-143 1.52e-24

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: 91.50  E-value: 1.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493    11 PRYPENGDEVFIRGKLKDDAKSFSVNFClprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQEEVlDNY 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQ---------CGPNADIALHFNPRFDEG----TIVRNsKQNGKWGKEER-SGG 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333470493    90 WHVDRSQTFRVVFRLHEDCIKVFVNsvDHPPdYQFPVQLPLDQIESIELWDDVE 143
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVN--GQHF-LEFPHRLPLESIDTLEISGDVQ 117
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-143 1.94e-14

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: 65.73  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493   5 PFTAKFPRYPENGDEVFIRGKLKDDAKSFSVNFclprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQE 83
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL----------GTGSSDIALHFNPRFDEN----VIVRNsFLNGNWGPE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493  84 EVlDNYWHVDRSQTFRVVFRLHEDCIKVFVNSVdhpPDYQFPVQLPLDQIESIELWDDVE 143
Cdd:cd00070   67 ER-SGGFPFQPGQPFELTILVEEDKFQIFVNGQ---HFFSFPHRLPLESIDYLSINGDVS 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 17-143 4.37e-14

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: 64.58  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493   17 GDEVFIRGKLKDDAKSFSVNFclprpaQVAEHQTPPyIALHFKTiydeRDDTSRVVLN-WKNLQWQQEEvldNYWH--VD 93
Cdd:pfam00337   7 GSSLTIKGIVLPDAQRFSINL------QTGVGPSDD-IALHFNP----RFDENVIVRNsRQNGQWGQEE---REGGfpFQ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 333470493   94 RSQTFRVVFRLHEDCIKVFVNSVdhpPDYQFPVQLPLDQIESIELWDDVE 143
Cdd:pfam00337  73 PGQPFELTILVGDDHFKIYVNGQ---HFTTFKHRLPPEDIDALQVRGDVK 119
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 11-143 1.52e-24

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: 91.50  E-value: 1.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493    11 PRYPENGDEVFIRGKLKDDAKSFSVNFClprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQEEVlDNY 89
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQ---------CGPNADIALHFNPRFDEG----TIVRNsKQNGKWGKEER-SGG 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 333470493    90 WHVDRSQTFRVVFRLHEDCIKVFVNsvDHPPdYQFPVQLPLDQIESIELWDDVE 143
Cdd:smart00908  67 FPFQPGQPFELEILVEEDEFKVAVN--GQHF-LEFPHRLPLESIDTLEISGDVQ 117
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 5-143 1.94e-14

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: 65.73  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493   5 PFTAKFPRYPENGDEVFIRGKLKDDAKSFSVNFclprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQE 83
Cdd:cd00070    1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINL----------GTGSSDIALHFNPRFDEN----VIVRNsFLNGNWGPE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493  84 EVlDNYWHVDRSQTFRVVFRLHEDCIKVFVNSVdhpPDYQFPVQLPLDQIESIELWDDVE 143
Cdd:cd00070   67 ER-SGGFPFQPGQPFELTILVEEDKFQIFVNGQ---HFFSFPHRLPLESIDYLSINGDVS 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 17-143 4.37e-14

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: 64.58  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493   17 GDEVFIRGKLKDDAKSFSVNFclprpaQVAEHQTPPyIALHFKTiydeRDDTSRVVLN-WKNLQWQQEEvldNYWH--VD 93
Cdd:pfam00337   7 GSSLTIKGIVLPDAQRFSINL------QTGVGPSDD-IALHFNP----RFDENVIVRNsRQNGQWGQEE---REGGfpFQ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 333470493   94 RSQTFRVVFRLHEDCIKVFVNSVdhpPDYQFPVQLPLDQIESIELWDDVE 143
Cdd:pfam00337  73 PGQPFELTILVGDDHFKIYVNGQ---HFTTFKHRLPPEDIDALQVRGDVK 119
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 6-150 6.51e-14

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 64.17  E-value: 6.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470493     6 FTAKFPRYPENGDEVFIRGKLKDDAKSFSVNFclprpaqvaeHQTPPYIALHFKTIYDERddtsRVVLN-WKNLQWQQEE 84
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINL----------LTGGDDIALHFNPRFNEN----KIVCNsKLNGSWGSEE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333470493    85 vLDNYWHVDRSQTFRVVFRLHEDCIKVFVNSVdhpPDYQFPVQLPLDQIESIELWDDVeHVEEISF 150
Cdd:smart00276  67 -REGGFPFQPGQPFDLTIIVQPDHFQIFVNGV---HITTFPHRLPLESIDYLSINGDV-QLTSVSF 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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