HAMAP rule MF_03115

General rule information [?]

Accession	MF_03115
Dates	11-FEB-2010 (Created) 19-NOV-2022 (Last updated, Version 16)
Name	Anamorsin
Scope(s)	Eukaryota Plastid
Template(s)	P36152 (DRE2_YEAST); Q6FI81 (CPIN1_HUMAN); Q8WTY4 (CPIN1_MOUSE); [ Recover all ]
Triggered by	HAMAP; MF_03115 (Get profile general information and statistics)

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	Name=DRE2;
else case <OC:Vertebrata>
Gene name	Name=CIAPIN1;
else case <OC:Drosophilidae>
Gene name	Name=CIAPIN1; Synonyms=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	Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
end case
case <FTGroup:3>
COFACTOR	Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
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.
DOMAIN	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 <OCellular component: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;
Pfam	PF08241; Methyltransf_11; 0-1;
Pfam	PF16803; DRE2_N; 0-1;

Features [?]

From: DRE2_YEAST (P36152)
Key	From	To	Description	Tag	Condition	FTGroup
REGION	1	158	/note="N-terminal SAM-like domain"
REGION	159	242	/note="Linker"
case <FTGroup:2>
REGION	252	268	/note="Fe-S binding site A"
end case
case <FTGroup:3>
REGION	311	325	/note="Fe-S binding site B"
end case
MOTIF	311	314	/note="Cx2C motif 1"		C-x(2)-C	1
MOTIF	322	325	/note="Cx2C motif 2"		C-x(2)-C	1
BINDING	252	252	/ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135"		C	2
BINDING	263	263	/ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135"		C	2
BINDING	266	266	/ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135"		C	2
BINDING	268	268	/ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135"		C	2
BINDING	311	311	/ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883"		C	3
BINDING	314	314	/ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883"		C	3
BINDING	322	322	/ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883"		C	3
BINDING	325	325	/ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883"		C	3

Additional information [?]

Size range	103-411 amino acids
Related rules	None
Fusion	Nter: None Cter: None

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