SMART: Pfam domain VOMI

The domain within your query sequence starts at position 35 and ends at position 199; the E-value for the VOMI domain shown below is 6.2e-64.

VDVTNGGTWGDWAWPEMCPDGYFASGFSVKVEPPQGIPGDDTALNGIRLHCTRGNSQKNT
HVVESQSGSWGSWSEPLWCPGTSFLVAFCLRVEPFTFPGDNTGVNNVRFRCSDGVELEGP
GLNWGDYGEWSNSCPKGVCGLQTKIQKPRGLRDDTALNDIRIFCC

VOMI

PFAM accession number:	PF03762
Interpro abstract (IPR005515):	Vitelline membrane outer layer protein I (VMO-I) is one of the proteins found in the outer layer of the vitelline membrane of eggs. VMO-I, lysozyme, and VMO-II are bound tightly to ovomucin fibrils of the egg yolk membrane. The structure of VMO-I [ (PUBMED:8131734) ] consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. It is a member of the beta-prism-fold family and the structure of VOM-I 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 [ (PUBMED:8848836) ]. VMO-I has been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine.

PFAM accession number:

PF03762

Interpro abstract (IPR005515):

Vitelline membrane outer layer protein I (VMO-I) is one of the proteins found in the outer layer of the vitelline membrane of eggs. VMO-I, lysozyme, and VMO-II are bound tightly to ovomucin fibrils of the egg yolk membrane. The structure of VMO-I [ (PUBMED:8131734) ] consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. It is a member of the beta-prism-fold family and the structure of VOM-I 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 [ (PUBMED:8848836) ]. VMO-I has been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry VOMI