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Conserved domains on  [gi|222144307|ref|NP_001138413|]
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vitelline membrane outer layer protein 1 homolog isoform 4 precursor [Homo sapiens]

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 ...
 36-65 7.72e-13

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 pfam03762:

Pssm-ID: 452732  Cd Length: 166  Bit Score: 59.21  E-value: 7.72e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 222144307   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIK 30
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 36-65 7.72e-13

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: 59.21  E-value: 7.72e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 222144307   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIK 30
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 35-65 2.35e-09

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: 50.08  E-value: 2.35e-09
                         10        20        30
                 ....*....|....*....|....*....|.
gi 222144307  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:cd00220    2 VIESPNGGNWGTWGQWERCPSGSFANGFQLK 32
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 36-65 7.72e-13

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: 59.21  E-value: 7.72e-13
                          10        20        30
                  ....*....|....*....|....*....|
gi 222144307   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIK 30
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 35-65 2.35e-09

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: 50.08  E-value: 2.35e-09
                         10        20        30
                 ....*....|....*....|....*....|.
gi 222144307  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:cd00220    2 VIESPNGGNWGTWGQWERCPSGSFANGFQLK 32
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 37-65 5.38e-04

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: 35.72  E-value: 5.38e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 222144307   37 EVTSG-GPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:pfam03762  60 NITSGeGFWGDWSGIQYCPAGGYLTGFQLR 89
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 37-65 2.71e-03

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: 33.90  E-value: 2.71e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 222144307  37 EVTSG-GPWGDWAWPEMCPDGFFASGFSLK 65
Cdd:cd00220   65 EIISGeGPWGSWREIQWCPNGTVIVGFALR 94
 
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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