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Conserved domains on  [gi|61888888|ref|NP_001013625|]
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vitelline membrane outer layer protein 1 homolog precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 35-199 2.36e-79

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: 234.09  E-value: 2.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888    35 VDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGIpGDDTALNGIRLHCTRGNSQKNTHVVESQSGSWGSWsEPLWCP 114
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888   115 GTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVELEGPGLNWGDYGEWS-NSCPKG--VCGLQTKIQKPRGLRDDTAL 191
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 61888888   192 NDIRIFCC 199
Cdd:pfam03762 159 NDVRFFCC 166
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 35-199 2.36e-79

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: 234.09  E-value: 2.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888    35 VDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGIpGDDTALNGIRLHCTRGNSQKNTHVVESQSGSWGSWsEPLWCP 114
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888   115 GTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVELEGPGLNWGDYGEWS-NSCPKG--VCGLQTKIQKPRGLRDDTAL 191
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 61888888   192 NDIRIFCC 199
Cdd:pfam03762 159 NDVRFFCC 166
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 33-199 1.67e-54

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: 171.42  E-value: 1.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888  33 SIVDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGiPGDDTALNGIRLHCTRGNSQKNT--HVVESQSGSWGSWSEP 110
Cdd:cd00220   1 TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGKTSNseNEIISGEGPWGSWREI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888 111 LWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVE----LEGPGLNWGDYGEWSNS--CPKG--VCGLQTKIQKP 182
Cdd:cd00220  80 QWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGrrkkTLSAEGDTNEWGSWTKDqfCPAGqaVCGIQTRIEPP 159

                       170
                ....*....|....*..
gi 61888888 183 RGLRDDTALNDIRIFCC 199
Cdd:cd00220 160 QGLGDDTALNNVNLKCC 176
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 35-199 2.36e-79

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: 234.09  E-value: 2.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888    35 VDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGIpGDDTALNGIRLHCTRGNSQKNTHVVESQSGSWGSWsEPLWCP 114
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888   115 GTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVELEGPGLNWGDYGEWS-NSCPKG--VCGLQTKIQKPRGLRDDTAL 191
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 61888888   192 NDIRIFCC 199
Cdd:pfam03762 159 NDVRFFCC 166
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 33-199 1.67e-54

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: 171.42  E-value: 1.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888  33 SIVDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGiPGDDTALNGIRLHCTRGNSQKNT--HVVESQSGSWGSWSEP 110
Cdd:cd00220   1 TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGKTSNseNEIISGEGPWGSWREI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888 111 LWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVE----LEGPGLNWGDYGEWSNS--CPKG--VCGLQTKIQKP 182
Cdd:cd00220  80 QWCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGrrkkTLSAEGDTNEWGSWTKDqfCPAGqaVCGIQTRIEPP 159

                       170
                ....*....|....*..
gi 61888888 183 RGLRDDTALNDIRIFCC 199
Cdd:cd00220 160 QGLGDDTALNNVNLKCC 176
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 28-87 3.75e-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: 53.55  E-value: 3.75e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 61888888  28 EPRYASIVDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGIpGDDTALNGIRLHCTR 87
Cdd:cd00220 119 GRRKKTLSAEGDTNEWGSWTKDQFCPAGQAVCGIQTRIEPPQGL-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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