DRE2_ENTBH
ID DRE2_ENTBH Reviewed; 103 AA.
AC B7XHF3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Fe-S cluster assembly protein DRE2;
DE AltName: Full=Anamorsin homolog;
GN Name=DRE2; ORFNames=EBI_27498;
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348;
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(2009).
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; ABGB01000014; EED44690.1; -; Genomic_DNA.
DR RefSeq; XP_002649460.1; XM_002649414.1.
DR AlphaFoldDB; B7XHF3; -.
DR STRING; 481877.B7XHF3; -.
DR EnsemblFungi; EED44690; EED44690; EBI_27498.
DR VEuPathDB; MicrosporidiaDB:EBI_27498; -.
DR HOGENOM; CLU_121509_2_0_1; -.
DR InParanoid; B7XHF3; -.
DR Proteomes; UP000001742; Unassembled WGS sequence.
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; IPR046408; CIAPIN1.
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..103
FT /note="Fe-S cluster assembly protein DRE2"
FT /id="PRO_0000392389"
FT REGION 19..103
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT REGION 42..55
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT REGION 70..84
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT MOTIF 70..73
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT MOTIF 81..84
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
SQ SEQUENCE 103 AA; 11764 MW; E6C710EA0FD66B77 CRC64;
MTSSDEELKE LLKQATTYKQ DPRHRIPMVD RPSKILTQSN KCRENKARKC SNCTCNKNTN
TNNTIYKSKC GSCHLGDPFR CSSCPYKGLP PFNEGDEINF DEL
