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Conserved domains on  [gi|1958659542|ref|XP_038942248|]
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vitelline membrane outer layer protein 1 homolog isoform X1 [Rattus norvegicus]

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 ...
 2-136 2.10e-58

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: 178.24  E-value: 2.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659542   2 VEPPQGIpGDDTALNGIRLHCTRGNAQQNTHVVESQSGSWGSWsEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFR 81
Cdd:pfam03762  31 VEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCPAGGYLTGFQLRVEPPQGIGDDTAANNIRFR 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659542  82 CSDGVELEGPGLNWGDYGEWS-DSCPKG--VCGLQTKIQKPRGLRDDTALNDVRIFCC 136
Cdd:pfam03762 109 CSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTALNDVRFFCC 166
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 2-136 2.10e-58

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: 178.24  E-value: 2.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659542   2 VEPPQGIpGDDTALNGIRLHCTRGNAQQNTHVVESQSGSWGSWsEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFR 81
Cdd:pfam03762  31 VEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCPAGGYLTGFQLRVEPPQGIGDDTAANNIRFR 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659542  82 CSDGVELEGPGLNWGDYGEWS-DSCPKG--VCGLQTKIQKPRGLRDDTALNDVRIFCC 136
Cdd:pfam03762 109 CSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTALNDVRFFCC 166
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 2-137 1.26e-38

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: 128.66  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659542   2 VEPPQGiPGDDTALNGIRLHCTRGNAQ--QNTHVVESQSGSWGSWSEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVR 79
Cdd:cd00220    33 YETPQG-FSDDTGLNAIALFCNPPDGKtsNSENEIISGEGPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFA 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659542  80 FRCSDGVE----LEGPGLNWGDYGEWSDS--CPKG--VCGLQTKIQKPRGLRDDTALNDVRIFCCN 137
Cdd:cd00220   112 AYCGRPEGrrkkTLSAEGDTNEWGSWTKDqfCPAGqaVCGIQTRIEPPQGLGDDTALNNVNLKCCR 177
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 2-136 2.10e-58

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: 178.24  E-value: 2.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659542   2 VEPPQGIpGDDTALNGIRLHCTRGNAQQNTHVVESQSGSWGSWsEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFR 81
Cdd:pfam03762  31 VEQPQGF-GDDTALNAIRLFCKPLDHDLNTNITSGEGFWGDWS-GIQYCPAGGYLTGFQLRVEPPQGIGDDTAANNIRFR 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659542  82 CSDGVELEGPGLNWGDYGEWS-DSCPKG--VCGLQTKIQKPRGLRDDTALNDVRIFCC 136
Cdd:pfam03762 109 CSNGEELEGDGNTWGDWGEWStDQCPGGtaICGIQTRVEPYQGGLDDTALNDVRFFCC 166
VMO-I cd00220
Vitelline membrane outer layer protein I (VMO-I) domain, VMO-I is one of the proteins found in ...
 2-137 1.26e-38

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: 128.66  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659542   2 VEPPQGiPGDDTALNGIRLHCTRGNAQ--QNTHVVESQSGSWGSWSEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVR 79
Cdd:cd00220    33 YETPQG-FSDDTGLNAIALFCNPPDGKtsNSENEIISGEGPWGSWREIQWCPNGTVIVGFALRSEPEQGKGDDTGANNFA 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659542  80 FRCSDGVE----LEGPGLNWGDYGEWSDS--CPKG--VCGLQTKIQKPRGLRDDTALNDVRIFCCN 137
Cdd:cd00220   112 AYCGRPEGrrkkTLSAEGDTNEWGSWTKDqfCPAGqaVCGIQTRIEPPQGLGDDTALNNVNLKCCR 177
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 92-135 5.31e-09

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: 51.51  E-value: 5.31e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958659542  92 GLNWGDYGEWsDSCPKG--VCGLQTKIQKPRGLRDDTALNDVRIFC 135
Cdd:pfam03762   6 GGNWGDWGPW-EMCPDGsfAYGFSIKVEQPQGFGDDTALNAIRLFC 50
 
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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