The domain within your query sequence starts at position 41 and ends at position 177; the E-value for the ApoO domain shown below is 3.3e-43.

SLYSVPEGQSKYVEEPRTQLEENISQLRHHCEPYTSFCQEIYSHTKPKVDHFVQWGVDNY
NYLQNAPPGFFPRLGVIGFAGFVGLLFARGSKIKKLVYPPFFMGLGASVYYPQQAITIAQ
ITGEKLYDWGLRGYIVI

ApoO

 ApoO
PFAM accession number:PF09769
Interpro abstract (IPR019166):

This entry includes MICOS complex subunit Mic26 from fungi and animals. Mammalian MIC26 and its paralogue, MIC27, can also be found in this entry. However, this entry does not include budding yeast Mic27.

Budding yeast Mic26 is a component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane [ (PUBMED:21987634) ].

Human MIC26 (also known as apolipoprotein O, APOO) plays a crucial role in crista junction formation and mitochondrial function [ (PUBMED:25764979) ] and can promote cardiac lipotoxicity by enhancing mitochondrial respiration and fatty acid metabolism in cardiac myoblasts [ (PUBMED:24743151) ]. It promotes cholesterol efflux from macrophage cells and can be detected in HDL, LDL and VLDL. It is secreted by a microsomal triglyceride transfer protein (MTTP)-dependent mechanism, probably as a VLDL-associated protein that is subsequently transferred to HDL [ (PUBMED:16956892) ].

Human MIC27 (also known as apolipoprotein O-like, APOOL) is also a subunit of the MICOS complex. It interacts with MIC26 and is involved in the formation of crista junctions [ (PUBMED:25764979) ].

GO process:cristae formation (GO:0042407)
GO component:MICOS complex (GO:0061617)

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