The domain within your query sequence starts at position 40 and ends at position 667; the E-value for the Mitofilin domain shown below is 3.6e-166.

GLTAGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFGMVLGSAPYTVPL
PKKPVQSGPLKISSVSEVMKDSKLPVAQSQKTKGDTPASAALAKSLEDALNRTSSVTLQT
ITAQNAAVQAVKAHSNILKTAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKA
KEELEKMKTIIEDAKKREIAGATPHITAAEGRLHNMIVDLDNVVKKVQAAQSEAKVVSQY
HELVVQARDDFRKELDSITPDITPGWKGMSISDLAGKLSTDDLNSLIAHAHRRIDQLNRE
LAQQKATEKQHIELALEKHKLEEKRTFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENE
MRTQLRRQAAAHTDHLRDVLKVQEQELKYEFEQGLSEKLSEQELEFRRRSQEQMDSFTLD
INTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAEMPTIPLGSAVEA
IRVNCSDNEFTQALTAAIPPESLTRGVYSEETLRARFYAVQKLARRVAMIDETRNSLYQY
FLSYLQSLLLFPPKQLKPPAELYPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESR
RVAQDWLKEARMTLETKQIVEILTAYAS

Mitofilin

Mitofilin
PFAM accession number:PF09731
Interpro abstract (IPR019133):

Mitofilin (also known as MICOS complex subunit MIC60) is a component of the MICOS complex which controls mitochondrial cristae morphology, maintenance of junctions, inner membrane architecture, and formation of contact sites to the outer membrane [ (PUBMED:22114354) (PUBMED:25781180) ]. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex [ (PUBMED:8886976) ]. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence (residues 1-43) rich in positive-charged and hydroxylated residues and a membrane anchor domain (residues 47-66). In addition, it has three centrally located coiled coil domains (residues 200-240, 280-310 and 400-420) [ (PUBMED:15647377) ].

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