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Conserved domains on  [gi|17565620|ref|NP_503538|]
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Vitelline membrane outer layer protein 1 [Caenorhabditis elegans]

Protein Classification

VMO-I domain-containing protein( domain architecture ID 10083057)

VMO-I domain-containing protein

Graphical summary

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List of domain hits

 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 ...
 20-196 2.15e-89

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: 265.41  E-value: 2.15e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620  20 VELRSPRYTNFGNWHPWSRCRDGEFAYGIQVKVEGDQRGGDDTGLNAVCLFCRPLGSDEISRENWINSGEGLWGVWGARK 99
Cdd:cd00220   1 TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQGFSDDTGLNAIALFCNPPDGKTSNSENEIISGEGPWGSWREIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620 100 YCQNTNVLIGFELRSEPDQRGKDDVAADNFAGYCGEPLGPRTKDVWVAGDTPGWGEWTGAQLCPERYAVCGIQSQIEGDQ 179
Cdd:cd00220  81 WCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAVCGIQTRIEPPQ 160

                       170
                ....*....|....*..
gi 17565620 180 RGGDDTALNNVNVECCK 196
Cdd:cd00220 161 GLGDDTALNNVNLKCCR 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 ...
 20-196 2.15e-89

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: 265.41  E-value: 2.15e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620  20 VELRSPRYTNFGNWHPWSRCRDGEFAYGIQVKVEGDQRGGDDTGLNAVCLFCRPLGSDEISRENWINSGEGLWGVWGARK 99
Cdd:cd00220   1 TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQGFSDDTGLNAIALFCNPPDGKTSNSENEIISGEGPWGSWREIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620 100 YCQNTNVLIGFELRSEPDQRGKDDVAADNFAGYCGEPLGPRTKDVWVAGDTPGWGEWTGAQLCPERYAVCGIQSQIEGDQ 179
Cdd:cd00220  81 WCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAVCGIQTRIEPPQ 160

                       170
                ....*....|....*..
gi 17565620 180 RGGDDTALNNVNVECCK 196
Cdd:cd00220 161 GLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 22-195 7.18e-82

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: 245.65  E-value: 7.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620    22 LRSPRYTNFGNWHPWSRCRDGEFAYGIQVKVEGDQRGGDDTGLNAVCLFCRPLGsdeISRENWINSGEGLWGVWGARKYC 101
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGFGDDTALNAIRLFCKPLD---HDLNTNITSGEGFWGDWSGIQYC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620   102 QNTNVLIGFELRSEPDQRGKDDVAADNFAGYCGEPLGprtkdvwVAGDTPG---WGEWTGAQlCPERYAVCGIQSQIEGD 178
Cdd:pfam03762  78 PAGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEE-------LEGDGNTwgdWGEWSTDQ-CPGGTAICGIQTRVEPY 149

                         170
                  ....*....|....*..
gi 17565620   179 QRGGDDTALNNVNVECC 195
Cdd:pfam03762 150 QGGLDDTALNDVRFFCC 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 ...
 20-196 2.15e-89

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: 265.41  E-value: 2.15e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620  20 VELRSPRYTNFGNWHPWSRCRDGEFAYGIQVKVEGDQRGGDDTGLNAVCLFCRPLGSDEISRENWINSGEGLWGVWGARK 99
Cdd:cd00220   1 TVIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQGFSDDTGLNAIALFCNPPDGKTSNSENEIISGEGPWGSWREIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620 100 YCQNTNVLIGFELRSEPDQRGKDDVAADNFAGYCGEPLGPRTKDVWVAGDTPGWGEWTGAQLCPERYAVCGIQSQIEGDQ 179
Cdd:cd00220  81 WCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGRRKKTLSAEGDTNEWGSWTKDQFCPAGQAVCGIQTRIEPPQ 160

                       170
                ....*....|....*..
gi 17565620 180 RGGDDTALNNVNVECCK 196
Cdd:cd00220 161 GLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 22-195 7.18e-82

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: 245.65  E-value: 7.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620    22 LRSPRYTNFGNWHPWSRCRDGEFAYGIQVKVEGDQRGGDDTGLNAVCLFCRPLGsdeISRENWINSGEGLWGVWGARKYC 101
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGFGDDTALNAIRLFCKPLD---HDLNTNITSGEGFWGDWSGIQYC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565620   102 QNTNVLIGFELRSEPDQRGKDDVAADNFAGYCGEPLGprtkdvwVAGDTPG---WGEWTGAQlCPERYAVCGIQSQIEGD 178
Cdd:pfam03762  78 PAGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEE-------LEGDGNTwgdWGEWSTDQ-CPGGTAICGIQTRVEPY 149

                         170
                  ....*....|....*..
gi 17565620   179 QRGGDDTALNNVNVECC 195
Cdd:pfam03762 150 QGGLDDTALNDVRFFCC 166
 
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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