NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32698964|ref|NP_872372|]
View 

vitelline membrane outer layer protein 1 homolog isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 36-200 9.76e-86

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: 250.27  E-value: 9.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964    36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHVvESQSGSWGEWSEPLWCR 115
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNI-TSGEGFWGDWSGIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964   116 GGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWS-DHCPKGA--CGLQTKIQGPRGLGDDTAL 192
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGTaiCGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 32698964   193 NDARLFCC 200
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 ...
 36-200 9.76e-86

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: 250.27  E-value: 9.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964    36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHVvESQSGSWGEWSEPLWCR 115
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNI-TSGEGFWGDWSGIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964   116 GGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWS-DHCPKGA--CGLQTKIQGPRGLGDDTAL 192
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGTaiCGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 32698964   193 NDARLFCC 200
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 ...
 35-201 1.58e-65

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: 199.54  E-value: 1.58e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGiPGDDTALNGIRLHCARGNV--LGNTHVVESQSGSWGEWSEPL 112
Cdd:cd00220   2 VIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGktSNSENEIISGEGPWGSWREIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964 113 WCRGGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEE----LQGPGLSWGDFGDWSD--HCPKG--ACGLQTKIQGPR 184
Cdd:cd00220  81 WCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGrrkkTLSAEGDTNEWGSWTKdqFCPAGqaVCGIQTRIEPPQ 160

                       170
                ....*....|....*..
gi 32698964 185 GLGDDTALNDARLFCCR 201
Cdd:cd00220 161 GLGDDTALNNVNLKCCR 177
 
Name Accession Description Interval E-value
VOMI pfam03762
Vitelline membrane outer layer protein I (VOMI); VOMI binds tightly to ovomucin fibrils of the ...
 36-200 9.76e-86

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: 250.27  E-value: 9.76e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964    36 IEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGIpGDDTALNGIRLHCARGNVLGNTHVvESQSGSWGEWSEPLWCR 115
Cdd:pfam03762   1 ITVPNGGNWGDWGPWEMCPDGSFAYGFSIKVEQPQGF-GDDTALNAIRLFCKPLDHDLNTNI-TSGEGFWGDWSGIQYCP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964   116 GGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEELQGPGLSWGDFGDWS-DHCPKGA--CGLQTKIQGPRGLGDDTAL 192
Cdd:pfam03762  79 AGGYLTGFQLRVEPPQGIGDDTAANNIRFRCSNGEELEGDGNTWGDWGEWStDQCPGGTaiCGIQTRVEPYQGGLDDTAL 158


                  ....*...
gi 32698964   193 NDARLFCC 200
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 ...
 35-201 1.58e-65

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: 199.54  E-value: 1.58e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964  35 VIEVTSGGPWGDWAWPEMCPDGFFASGFSLKVEPPQGiPGDDTALNGIRLHCARGNV--LGNTHVVESQSGSWGEWSEPL 112
Cdd:cd00220   2 VIESPNGGNWGTWGQWERCPSGSFANGFQLKYETPQG-FSDDTGLNAIALFCNPPDGktSNSENEIISGEGPWGSWREIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32698964 113 WCRGGAYLVAFSLRVEAPTTLGDNTAANNVRFRCSDGEE----LQGPGLSWGDFGDWSD--HCPKG--ACGLQTKIQGPR 184
Cdd:cd00220  81 WCPNGTVIVGFALRSEPEQGKGDDTGANNFAAYCGRPEGrrkkTLSAEGDTNEWGSWTKdqFCPAGqaVCGIQTRIEPPQ 160

                       170
                ....*....|....*..
gi 32698964 185 GLGDDTALNDARLFCCR 201
Cdd:cd00220 161 GLGDDTALNNVNLKCCR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH