The domain within your query sequence starts at position 29 and ends at position 158; the E-value for the Ephrin domain shown below is 4.5e-42.

ADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYS
ACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGR
RSCLKLKVFV

Ephrin

Ephrin
PFAM accession number:PF00812
Interpro abstract (IPR001799):

Ephrins are a family of proteins [ (PUBMED:7838529) ] that are ligands of class V (EPH-related) receptor protein-tyrosine kinases. Initially identified as regulators of axon pathfinding and neuronal cell migration, the Eph receptors and their ephrin ligands are now known to have roles in many other cell-cell interactions, including those of vascular endothelial cells and specialised epithelia [ (PUBMED:11780069) ].

Ephrins are membrane-attached proteins of 205 to 340 residues. Attachment appears to be crucial for their normal function. Type-A ephrins are linked to the membrane via a GPI linkage, while type-B ephrins are type-I membrane proteins.

The globular ephrin receptor-binding domain (ephrin RBD) is a beta barrel composed of eight strands arranged in two sheets around a hydrophobic core. Interspersed between beta strands are two alpha helices and one 3(10) helix. The sheets are composed of mixed parallel and antiparallel beta strands arranged in a Greek key topology. Like other cell-surface proteins, ephrins contain disulfide bonds to enhance stability. Two buried disulfide bonds are present: one pair holds together beta strands C and F, and the other pair anchors two small helices, E and I, at the top of the barrel [ (PUBMED:11780069) (PUBMED:11703926) ].

GO component:membrane (GO:0016020)

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