Home  |  Contact
Annotation rule MF_03115
Send feedback

General rule information [?]

Accession MF_03115
Dates 11-FEB-2010 (Created)
16-FEB-2021 (Last updated, Version 13)
Name Anamorsin
Scope
Eukaryota
Plastid
Templates P36152 (DRE2_YEAST); Q6FI81 (CPIN1_HUMAN); Q8WTY4 (CPIN1_MOUSE): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

case <OC:Vertebrata>
Identifier
CPIN1
else
Identifier
DRE2
end case
case <OC:Fungi>
Protein name
RecName: Full=Fe-S cluster assembly protein ;
AltName: Full=Anamorsin homolog;
else case <OC:Vertebrata>
Protein name
RecName: Full=Anamorsin;
AltName: Full=Cytokine-induced apoptosis inhibitor 1;
AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
else
Protein name
RecName: Full=Anamorsin homolog;
AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
end case
case <OC:Fungi>
Gene name
DRE2
else case <OC:Vertebrata>
Gene name
CIAPIN1
else case <OC:Drosophilidae>
Gene name
CIAPIN1, l(2)35Bg
end case

Comments [?]

case <OC:Fungi>
Function Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Subunit Monomer. Interacts with @gn(TAH18). Interacts with @gn(MIA40).
else case <OC:Vertebrata>
Function Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells.
Subunit Monomer. Interacts with @gn(NDOR1). Interacts with @gn(CHCHD4).
else
Function Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subunit Monomer.
end case
case <FTGroup:2>
Cofactor [2Fe-2S] cluster
end case
case <FTGroup:3>
Cofactor [4Fe-4S] cluster
end case
case <OC:Vertebrata>
Subcellular location Cytoplasm. Nucleus. Mitochondrion intermembrane space.
else
Subcellular location Cytoplasm. Mitochondrion intermembrane space.
end case
Domain The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
case <OC:Vertebrata> and <FTGroup:1>
Domain The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
else case <FTGroup:1>
Domain The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
end case
Similarity Belongs to the anamorsin family.

Keywords [?]

case <FTGroup:2>
2Fe-2S
end case
case <FTGroup:3>
4Fe-4S
end case
Cytoplasm
Iron
Iron-sulfur
Metal-binding
Mitochondrion
case <OC:Vertebrata>
Apoptosis
Nucleus
end case

Gene Ontology [?]

GO:0005737; Cellular component: cytoplasm.
GO:0005758; Cellular component: mitochondrial intermembrane space.
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding.
GO:0009055; Molecular function: electron transfer activity.
GO:0016226; Biological process: iron-sulfur cluster assembly.
case <OC:Vertebrata>
GO:0005634; Cellular component: nucleus.
GO:0043066; Biological process: negative regulation of apoptotic process.
GO:0030097; Biological process: hemopoiesis.
end case

Cross-references [?]

Pfam PF05093; CIAPIN1; 1;
PF08241; Methyltransf_11; 0-1;
PF16803; DRE2_N; 0-1;

Features [?]

From: DRE2_YEAST (P36152)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     1     158       N-terminal SAM-like domain        
REGION     159     242       Linker        
case <FTGroup:2>
REGION     252     268       Fe-S binding site A        
end case
case <FTGroup:3>
REGION     311     325       Fe-S binding site B        
end case
MOTIF     311     314       Cx2C motif 1     C-x(2)-C   1
MOTIF     322     325       Cx2C motif 2     C-x(2)-C   1
METAL     252     252       Iron-sulfur (2Fe-2S)     C   2
METAL     263     263       Iron-sulfur (2Fe-2S)     C   2
METAL     266     266       Iron-sulfur (2Fe-2S)     C   2
METAL     268     268       Iron-sulfur (2Fe-2S)     C   2
METAL     311     311       Iron-sulfur (4Fe-4S)     C   3
METAL     314     314       Iron-sulfur (4Fe-4S)     C   3
METAL     322     322       Iron-sulfur (4Fe-4S)     C   3
METAL     325     325       Iron-sulfur (4Fe-4S)     C   3

Additional information [?]

Size range 103-411 amino acids
Related rules None
Fusion None


View rule in raw text format (no links)