AC   MF_03115;
DC   Protein; auto
TR   HAMAP; MF_03115; -; 1; level=0
XX
Names: Anamorsin
XX
case <OC:Vertebrata>
ID   CPIN1
else
ID   DRE2
end case
case <OC:Fungi>
DE   RecName: Full=Fe-S cluster assembly protein <gene_name>;
DE   AltName: Full=Anamorsin homolog;
else case <OC:Vertebrata>
DE   RecName: Full=Anamorsin;
DE   AltName: Full=Cytokine-induced apoptosis inhibitor 1;
DE   AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
else
DE   RecName: Full=Anamorsin homolog;
DE   AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
end case
case <OC:Fungi>
GN   Name=DRE2;
else case <OC:Vertebrata>
GN   Name=CIAPIN1;
else case <OC:Drosophilidae>
GN   Name=CIAPIN1; Synonyms=l(2)35Bg;
end case
XX
case <OC:Fungi>
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC       assembly (CIA) machinery required for the maturation of
CC       extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC       functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC       the de novo assembly of a [4Fe-4S] cluster on the scaffold complex
CC       CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the
CC       FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for
CC       the assembly of the diferric tyrosyl radical cofactor of ribonucleotide
CC       reductase (RNR), probably by providing electrons for reduction during
CC       radical cofactor maturation in the catalytic small subunit RNR2.
CC   -!- SUBUNIT: Monomer. Interacts with @gn(TAH18). Interacts with @gn(MIA40).
else case <OC:Vertebrata>
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC       assembly (CIA) machinery required for the maturation of
CC       extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC       functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC       the de novo assembly of a [4Fe-4S] cluster on the scaffold complex
CC       NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the
CC       FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required
CC       for the assembly of the diferric tyrosyl radical cofactor of
CC       ribonucleotide reductase (RNR), probably by providing electrons for
CC       reduction during radical cofactor maturation in the catalytic small
CC       subunit. Has anti-apoptotic effects in the cell. Involved in negative
CC       control of cell death upon cytokine withdrawal. Promotes development of
CC       hematopoietic cells.
CC   -!- SUBUNIT: Monomer. Interacts with @gn(NDOR1). Interacts with
CC       @gn(CHCHD4).
else
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC       assembly (CIA) machinery. Required for the maturation of
CC       extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC       functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC       the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S
CC       scaffold complex. Electrons are transferred from NADPH via a FAD- and
CC       FMN-containing diflavin oxidoreductase. Together with the diflavin
CC       oxidoreductase, also required for the assembly of the diferric tyrosyl
CC       radical cofactor of ribonucleotide reductase (RNR), probably by
CC       providing electrons for reduction during radical cofactor maturation in
CC       the catalytic small subunit.
CC   -!- SUBUNIT: Monomer.
end case
case <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
end case
case <FTGroup:3>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
end case
case <OC:Vertebrata>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion intermembrane
CC       space.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space.
end case
CC   -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC       adenosyl-L-methionine-dependent methyltransferases, but does not bind
CC       S-adenosyl-L-methionine. It is required for correct assembly of the 2
CC       Fe-S clusters.
CC   -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC       mostly in an intrinsically disordered conformation.
case <OC:Vertebrata> and <FTGroup:1>
CC   -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC       mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The
CC       formation of 2 disulfide bonds in the Cx2C motifs through
CC       dithiol/disulfide exchange reactions effectively traps the protein in
CC       the mitochondrial intermembrane space.
else case <FTGroup:1>
CC   -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC       mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2
CC       disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange
CC       reactions effectively traps the protein in the mitochondrial
CC       intermembrane space.
end case
CC   -!- SIMILARITY: Belongs to the anamorsin family.
XX
DR   Pfam; PF05093; CIAPIN1; 1; trigger=no
DR   Pfam; PF08241; Methyltransf_11; 0-1; trigger=no
DR   Pfam; PF16803; DRE2_N; 0-1; trigger=no
XX
case <FTGroup:2>
KW   2Fe-2S
end case
case <FTGroup:3>
KW   4Fe-4S
end case
KW   Cytoplasm
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
KW   Mitochondrion
case <OC:Vertebrata>
KW   Apoptosis
KW   Nucleus
end case
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0005758; C:mitochondrial intermembrane space
GO   GO:0051537; F:2 iron, 2 sulfur cluster binding
GO   GO:0009055; F:electron transfer activity
GO   GO:0016226; P:iron-sulfur cluster assembly
case <OC:Vertebrata>
GO   GO:0005634; C:nucleus
GO   GO:0043066; P:negative regulation of apoptotic process
GO   GO:0030097; P:hemopoiesis
end case
XX
FT   From: DRE2_YEAST (P36152)
FT   REGION          1..158
FT                   /note="N-terminal SAM-like domain"
FT   REGION          159..242
FT                   /note="Linker"
case <FTGroup:2>
FT   REGION          252..268
FT                   /note="Fe-S binding site A"
end case
case <FTGroup:3>
FT   REGION          311..325
FT                   /note="Fe-S binding site B"
end case
FT   MOTIF           311..314
FT                   /note="Cx2C motif 1"
FT   Group: 1; Condition: C-x(2)-C
FT   MOTIF           322..325
FT                   /note="Cx2C motif 2"
FT   Group: 1; Condition: C-x(2)-C
FT   BINDING         252
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Group: 2; Condition: C
FT   BINDING         263
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Group: 2; Condition: C
FT   BINDING         266
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Group: 2; Condition: C
FT   BINDING         268
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Group: 2; Condition: C
FT   BINDING         311
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 3; Condition: C
FT   BINDING         314
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 3; Condition: C
FT   BINDING         322
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 3; Condition: C
FT   BINDING         325
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 3; Condition: C
XX
Size: 103-411;
Related: None;
Template: P36152; Q6FI81; Q8WTY4;
Scope:
 Eukaryota
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in CANAL, ORYSI, ORYSJ, PARTE, PHYPA, PICSI, SALSA, TOXGO, TRYCR
Plasmid: None
Comments: None
XX
# Revision 1.16 2022/11/19
//