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Conserved domains on  [gi|222144303|ref|NP_001138411|]
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vitelline membrane outer layer protein 1 homolog isoform 2 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 ...
 36-106 3.57e-29

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: 103.13  E-value: 3.57e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222144303   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHvVESQSGRWG 106
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTN-ITSGEGFWG 69
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 36-106 3.57e-29

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: 103.13  E-value: 3.57e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222144303   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHvVESQSGRWG 106
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTN-ITSGEGFWG 69
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 35-106 3.97e-23

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: 87.83  E-value: 3.97e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222144303  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGiPGDDTALNGIRLHCARGNV--LGNTHVVESQSGRWG 106
Cdd:cd00220    2 VIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGktSNSENEIISGEGPWG 74
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 36-106 3.57e-29

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: 103.13  E-value: 3.57e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222144303   36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHvVESQSGRWG 106
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTN-ITSGEGFWG 69
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 35-106 3.97e-23

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: 87.83  E-value: 3.97e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222144303  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGiPGDDTALNGIRLHCARGNV--LGNTHVVESQSGRWG 106
Cdd:cd00220    2 VIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGktSNSENEIISGEGPWG 74
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 37-92 1.22e-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: 65.76  E-value: 1.22e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 222144303   37 EVTSG-GPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVL 92
Cdd:pfam03762  60 NITSGeGFWGDWSGIQYCPAGGYLTGFQLRVEPPQGI-GDDTAANNIRFRCSNGEEL 115
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 37-106 2.79e-12

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: 59.71  E-value: 2.79e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222144303  37 EVTSG-GPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGN-THVVESQSGRWG 106
Cdd:cd00220   65 EIISGeGPWGSWREIQWCPNGTVIVGFALRSEPEQGK-GDDTGANNFAAYCGRPEGRRKkTLSAEGDTNEWG 135
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 21-86 5.21e-10

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: 53.44  E-value: 5.21e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222144303   21 FTCAQTDGRNGYTavievTSGGPWGDWAwPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHC 86
Cdd:pfam03762 107 FRCSNGEELEGDG-----NTWGDWGEWS-TDQCPGGTAICGIQTRVEPYQGG-LDDTALNDVRFFC 165
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 21-88 1.58e-08

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: 49.70  E-value: 1.58e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222144303  21 FTCAQTDGRNGYTAVIEvTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCAR 88
Cdd:cd00220  112 AYCGRPEGRRKKTLSAE-GDTNEWGSWTKDQFCPAGQAVCGIQTRIEPPQGL-GDDTALNNVNLKCCR 177
 
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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