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Annotation rule MF_03115 |
General rule information
[?]
Accession |
MF_03115 |
Dates |
11-FEB-2010 (Created) 20-NOV-2019 (Last updated, Version 11) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Vertebrata>
else
end case
case <OC:Fungi>
Protein name |
RecName:
|
Full=Fe-S cluster assembly protein ;
|
AltName:
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Full=Anamorsin homolog;
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|
else case <OC:Vertebrata>
Protein name |
RecName:
|
Full=Anamorsin;
|
AltName:
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Full=Cytokine-induced apoptosis inhibitor 1;
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AltName:
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Full=Fe-S cluster assembly protein DRE2 homolog;
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|
else
Protein name |
RecName:
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Full=Anamorsin homolog;
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AltName:
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Full=Fe-S cluster assembly protein DRE2 homolog;
|
|
end case
case <OC:Fungi>
else case <OC:Vertebrata>
else case <OC:Drosophilidae>
end case
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>
end case
case <FTGroup:3>
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. |
case <FTGroup:2>
end case
case <FTGroup:3>
end case
case <OC:Vertebrata>
end case
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
From: DRE2_YEAST (P36152) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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REGION
|
|
1
|
|
158
|
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N-terminal SAM-like domain
|
|
|
|
|
|
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REGION
|
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159
|
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242
|
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Linker
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|
|
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REGION
|
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243
|
|
Cter
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Intrinsically disordered
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case <FTGroup:2>
REGION
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252
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268
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Fe-S binding site A
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|
|
|
|
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|
end case
case <FTGroup:3>
REGION
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311
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325
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Fe-S binding site B
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end case
MOTIF
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311
|
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314
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Cx2C motif 1
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C-x(2)-C
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1
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MOTIF
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322
|
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325
|
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Cx2C motif 2
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C-x(2)-C
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1
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METAL
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252
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252
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Iron-sulfur (2Fe-2S)
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|
|
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C
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2
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METAL
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263
|
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263
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Iron-sulfur (2Fe-2S)
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|
|
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C
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2
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METAL
|
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266
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266
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Iron-sulfur (2Fe-2S)
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|
|
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C
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2
|
METAL
|
|
268
|
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268
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Iron-sulfur (2Fe-2S)
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|
|
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C
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2
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METAL
|
|
311
|
|
311
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Iron-sulfur (4Fe-4S)
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|
|
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C
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3
|
METAL
|
|
314
|
|
314
|
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Iron-sulfur (4Fe-4S)
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|
|
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C
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3
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METAL
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322
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322
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Iron-sulfur (4Fe-4S)
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|
|
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C
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3
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METAL
|
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325
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325
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Iron-sulfur (4Fe-4S)
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C
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3
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Additional information
[?]
Size range |
103-411 amino acids |
Related rules |
None |
Fusion |
None |