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DRE2_CANAW
ID   DRE2_CANAW              Reviewed;         411 AA.
AC   C4YL88;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Fe-S cluster assembly protein DRE2 {ECO:0000255|HAMAP-Rule:MF_03115};
DE   AltName: Full=Anamorsin homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN   Name=DRE2 {ECO:0000255|HAMAP-Rule:MF_03115}; ORFNames=CAWG_01605;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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:0000255|HAMAP-Rule:MF_03115}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- SUBUNIT: Monomer. Interacts with TAH18. Interacts with MIA40.
CC       {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}.
CC       Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC       mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP-
CC       Rule:MF_03115}.
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. {ECO:0000255|HAMAP-Rule:MF_03115}.
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:0000255|HAMAP-Rule:MF_03115}.
CC   -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC       Rule:MF_03115}.
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DR   EMBL; CM000309; EEQ43369.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YL88; -.
DR   SMR; C4YL88; -.
DR   STRING; 5476.C4YL88; -.
DR   EnsemblFungi; EEQ43369; EEQ43369; CAWG_01605.
DR   VEuPathDB; FungiDB:CAWG_01605; -.
DR   HOGENOM; CLU_067152_0_0_1; -.
DR   OMA; TMITCGK; -.
DR   Proteomes; UP000001429; Chromosome R.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03115; Anamorsin; 1.
DR   InterPro; IPR007785; Anamorsin.
DR   InterPro; IPR046408; CIAPIN1.
DR   InterPro; IPR031838; Dre2_N.
DR   PANTHER; PTHR13273; PTHR13273; 1.
DR   Pfam; PF05093; CIAPIN1; 1.
DR   Pfam; PF16803; DRE2_N; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion.
FT   CHAIN           1..411
FT                   /note="Fe-S cluster assembly protein DRE2"
FT                   /id="PRO_0000392380"
FT   REGION          1..192
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          190..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..261
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          281..300
FT                   /note="Fe-S binding site A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          374..388
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           374..377
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           385..388
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   COMPBIAS        196..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         281
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         295
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         298
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         300
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         374
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         377
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         385
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         388
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ   SEQUENCE   411 AA;  46144 MW;  BA9481978C3EFFBC CRC64;
     MTSSINILLL LHPTVVTDAQ LVEQIKSKIY QSHNNNNNNN GGTTTTTTGT VNINLNQQII
     DRVTKGIIEL PYDYYDEIIY INPNNESQYR EIPISLMQLI YKLLKSNGKF KGDLPLDQNL
     DVLMTGFIIE EEEKEKEENN LEGELVNVWV KPIPVDEPVV TLLKKKTTTS NTTTKKKSLP
     LFKKLNKDEI NNSDKDINND NITNNNNNNN NNKRKLVETK LTYFSSDDEN SSDGSVSEND
     DIDDDDELID ENDLLNFNNN NNNNTNGGSL LSDKLITPRK CDISLNGGKK RKKACKDCTC
     GLKELEELEV SNQQNLQDQI LGKLAQSATL EAIKIEERLK QQQQQQQQQK VKVKFTEEDL
     SEIDFTVQGK TGGCGSCALG DAFRCDGCPY LGLPPFKPGE VVKLDGFGED I
 
 
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