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Conserved domains on  [gi|453232666|ref|NP_001263915|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VMO-I super family cl27236
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 28-79 1.80e-16

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


The actual alignment was detected with superfamily member cd00220:

Pssm-ID: 452732  Cd Length: 177  Bit Score: 69.34  E-value: 1.80e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 453232666  28 LGSPRVNNQGTWKAWQICHDGWFVHGMQLKYEAT--GGDLTGMNAVALYCQRIG 79
Cdd:cd00220    3 IESPNGGNWGTWGQWERCPSGSFANGFQLKYETPqgFSDDTGLNAIALFCNPPD 56
 
Name Accession Description Interval E-value
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 28-79 1.80e-16

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


Pssm-ID: 238135  Cd Length: 177  Bit Score: 69.34  E-value: 1.80e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 453232666  28 LGSPRVNNQGTWKAWQICHDGWFVHGMQLKYEAT--GGDLTGMNAVALYCQRIG 79
Cdd:cd00220    3 IESPNGGNWGTWGQWERCPSGSFANGFQLKYETPqgFSDDTGLNAIALFCNPPD 56
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 30-75 1.86e-14

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 63.84  E-value: 1.86e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 453232666   30 SPRVNNQGTWKAWQICHDGWFVHGMQLKYEA--TGGDLTGMNAVALYC 75
Cdd:pfam03762   3 VPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQpqGFGDDTALNAIRLFC 50
 
Name Accession Description Interval E-value
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 28-79 1.80e-16

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


Pssm-ID: 238135  Cd Length: 177  Bit Score: 69.34  E-value: 1.80e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 453232666  28 LGSPRVNNQGTWKAWQICHDGWFVHGMQLKYEAT--GGDLTGMNAVALYCQRIG 79
Cdd:cd00220    3 IESPNGGNWGTWGQWERCPSGSFANGFQLKYETPqgFSDDTGLNAIALFCNPPD 56
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 30-75 1.86e-14

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 63.84  E-value: 1.86e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 453232666   30 SPRVNNQGTWKAWQICHDGWFVHGMQLKYEA--TGGDLTGMNAVALYC 75
Cdd:pfam03762   3 VPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQpqGFGDDTALNAIRLFC 50
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 37-77 2.82e-04

Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in the outer layer of the vitelline membrane of poultry eggs; VMO-I, lysozyme, and VMO-II are tightly bound to ovomucin; this complex forms the backbone of the outer layer; VMO-I has three distinct internal repeats; all three repeats are used to define the domain here; VMO-I has recently been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine; may be a carbohydrate-binding protein; member of the beta-prism-fold family


Pssm-ID: 238135  Cd Length: 177  Bit Score: 36.98  E-value: 2.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 453232666  37 GTWKAWQICHDGWFVHGMQLKYEA--TGGDLTGMNAVALYCQR 77
Cdd:cd00220   74 GSWREIQWCPNGTVIVGFALRSEPeqGKGDDTGANNFAAYCGR 116
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 37-75 1.51e-03

Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold.


Pssm-ID: 427492  Cd Length: 166  Bit Score: 34.95  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 453232666   37 GTWKAWQICHDGWFVHGMQLKYEA--TGGDLTGMNAVALYC 75
Cdd:pfam03762  69 GDWSGIQYCPAGGYLTGFQLRVEPpqGIGDDTAANNIRFRC 109
 
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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