The domain within your query sequence starts at position 91 and ends at position 252; the E-value for the GIDE domain shown below is 1e-26.

LQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETV
YEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQ
GMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFF

GIDE

 GIDE
PFAM accession number:PF12483
Interpro abstract (IPR022170):

This family includes mitochondrial ubiquitin ligase activator of NFKB 1 (MULAN, also known as MUL1) from animals and ubiquitin E3 Ligase SP1/SP2/SPL1/SPL2 from Arabidopsis.

MUL1 is a multifunctional E3 ubiquitin ligase anchored in the outer mitochondrial membrane with its RING finger domain facing the cytoplasm. Mul1 functions as a ubiquitin ligase to ubiquitinate molecules such as mitofusin2 (Mfn2), Akt, p53 and ULK1, through its RING finger domain, leading to proteins degradation. Moreover, Mul1 can also act as a small ubiquitin-like modifiers (SUMO) E3 ligase to sumoylate proteins such as dynamin-related protein 1 (Drp1), enhancing protein stabilization [ (PUBMED:27034206) ]. It plays a role in the control of mitochondrial morphology, promotes mitochondrial fragmentation and influences mitochondrial localisation [ (PUBMED:18207745) ]. When over-expressed in human cells, it activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis [ (PUBMED:18591963) ]. MUL1 has also been shown to regulate RIG-I mediated antiviral response [ (PUBMED:23399697) ].

Ubiquitin E3 ligase SP1 associates with TOC (translocon at the outer envelope membrane of chloroplasts) complexes and mediates ubiquitination of TOC components, promoting their degradation. SP1-mediated regulation of chloroplast protein import contributes to the organellar proteome changes that occur during plant development [ (PUBMED:23118188) ]. It is also important for stress tolerance in plants [ (PUBMED:26387714) ].

GO process:protein ubiquitination (GO:0016567), organelle organization (GO:0006996)
GO function:ubiquitin-protein transferase activity (GO:0004842)

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