ID   DRE2_ENCCU              Reviewed;         112 AA.
AC   Q8SWE5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Fe-S cluster assembly protein DRE2;
DE   AltName: Full=Anamorsin homolog;
GN   Name=DRE2; OrderedLocusNames=ECU02_0490;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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       {ECO:0000250|UniProtKB:P36152}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P36152};
CC   -!- SUBUNIT: Monomer. Interacts with TAH18. Interacts with MIA40.
CC       {ECO:0000250|UniProtKB:P36152}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36152}.
CC       Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P36152}.
CC   -!- DOMAIN: The C-terminal domain binds 1 Fe-S cluster but is otherwise
CC       mostly in an intrinsically disordered conformation.
CC       {ECO:0000250|UniProtKB:P36152}.
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. {ECO:0000250|UniProtKB:P36152}.
CC   -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000305}.
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DR   EMBL; AL590442; CAD25080.1; -; Genomic_DNA.
DR   RefSeq; NP_584576.1; NM_001040765.1.
DR   AlphaFoldDB; Q8SWE5; -.
DR   STRING; 284813.Q8SWE5; -.
DR   PRIDE; Q8SWE5; -.
DR   GeneID; 858566; -.
DR   KEGG; ecu:ECU02_0490; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_0490; -.
DR   HOGENOM; CLU_121509_2_0_1; -.
DR   InParanoid; Q8SWE5; -.
DR   OMA; KMQDEYL; -.
DR   OrthoDB; 1588798at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   InterPro; IPR007785; Anamorsin.
DR   InterPro; IPR046408; CIAPIN1.
DR   PANTHER; PTHR13273; PTHR13273; 1.
DR   Pfam; PF05093; CIAPIN1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome.
FT   CHAIN           1..112
FT                   /note="Fe-S cluster assembly protein DRE2"
FT                   /id="PRO_0000392388"
FT   REGION          8..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   REGION          69..83
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   MOTIF           69..72
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   MOTIF           80..83
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   BINDING         72
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
SQ   SEQUENCE   112 AA;  12722 MW;  0D632D468A24BB39 CRC64;
     MEDKEELRKL LRSMMRKSTD PRTKMQDEYL TDEDKAIQRS ERPPAKKRAC KDCTCGLKEE
     QEVRTRSACG NCYKGDAFRC SGCPSLGLPP YEPGDVVSFS MDLSNEFQGE DA