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Conserved domains on  [gi|392889018|ref|NP_493814|]
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Vitelline membrane outer layer protein 1 homolog [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 ...
 3-110 5.03e-42

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: 135.98  E-value: 5.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889018   3 EGPFGKWYDFQYCPNNLVIVGFRLKSERQSNAVDDAGALNIAVFCGTPNHRGHIVTLEGEVNIKSGKWTADQFCPSNFAV 82
Cdd:cd00220   70 EGPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                         90       100
                 ....*....|....*....|....*...
gi 392889018  83 CGIRTQIEKDQEEGDDTGLNNVQMNCCP 110
Cdd:cd00220  150 CGIQTRIEPPQGLGDDTALNNVNLKCCR 177
 
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 ...
 3-110 5.03e-42

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: 135.98  E-value: 5.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889018   3 EGPFGKWYDFQYCPNNLVIVGFRLKSERQSNAVDDAGALNIAVFCGTPNHRGHIVTLEGEVNIKSGKWTADQFCPSNFAV 82
Cdd:cd00220   70 EGPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                         90       100
                 ....*....|....*....|....*...
gi 392889018  83 CGIRTQIEKDQEEGDDTGLNNVQMNCCP 110
Cdd:cd00220  150 CGIQTRIEPPQGLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 2-109 1.29e-34

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: 116.99  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889018    2 REGPFGKWYDFQYCPNNLVIVGFRLKSERQSNAVDDAGALNIAVFCGTPNhrghivTLEGEVNIKS--GKWTADQfCPSN 79
Cdd:pfam03762  64 GEGFWGDWSGIQYCPAGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGE------ELEGDGNTWGdwGEWSTDQ-CPGG 136

                          90       100       110
                  ....*....|....*....|....*....|
gi 392889018   80 FAVCGIRTQIEKDQEEGDDTGLNNVQMNCC 109
Cdd:pfam03762 137 TAICGIQTRVEPYQGGLDDTALNDVRFFCC 166
 
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 ...
 3-110 5.03e-42

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: 135.98  E-value: 5.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889018   3 EGPFGKWYDFQYCPNNLVIVGFRLKSERQSNAVDDAGALNIAVFCGTPNHRGHIVTLEGEVNIKSGKWTADQFCPSNFAV 82
Cdd:cd00220   70 EGPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAV 149

                         90       100
                 ....*....|....*....|....*...
gi 392889018  83 CGIRTQIEKDQEEGDDTGLNNVQMNCCP 110
Cdd:cd00220  150 CGIQTRIEPPQGLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 2-109 1.29e-34

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: 116.99  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889018    2 REGPFGKWYDFQYCPNNLVIVGFRLKSERQSNAVDDAGALNIAVFCGTPNhrghivTLEGEVNIKS--GKWTADQfCPSN 79
Cdd:pfam03762  64 GEGFWGDWSGIQYCPAGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGE------ELEGDGNTWGdwGEWSTDQ-CPGG 136

                          90       100       110
                  ....*....|....*....|....*....|
gi 392889018   80 FAVCGIRTQIEKDQEEGDDTGLNNVQMNCC 109
Cdd:pfam03762 137 TAICGIQTRVEPYQGGLDDTALNDVRFFCC 166
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 68-112 1.45e-07

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: 46.89  E-value: 1.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 392889018   68 GKWTADQFCPSNFAVCGIRTQIEKDQEEGDDTGLNNVQMNCCPVD 112
Cdd:pfam03762  10 GDWGPWEMCPDGSFAYGFSIKVEQPQGFGDDTALNAIRLFCKPLD 54
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 68-112 8.77e-05

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: 39.68  E-value: 8.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 392889018  68 GKWTADQFCPSNFAVCGIRTQIEKDQEEGDDTGLNNVQMNCCPVD 112
Cdd:cd00220   12 GTWGQWERCPSGSFANGFQLKYETPQGFSDDTGLNAIALFCNPPD 56
 
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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