ID   DRE2_LODEL              Reviewed;         313 AA.
AC   A5DRX1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Fe-S cluster assembly protein DRE2;
DE   AltName: Full=Anamorsin homolog;
GN   Name=DRE2; ORFNames=LELG_00107;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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: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 2 Fe-S clusters but is otherwise
CC       mostly in an intrinsically disordered conformation.
CC       {ECO:0000250|UniProtKB:P36152}.
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:0000250|UniProtKB:P36152}.
CC   -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000305}.
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DR   EMBL; CH981524; EDK41929.1; -; Genomic_DNA.
DR   RefSeq; XP_001527587.1; XM_001527537.1.
DR   AlphaFoldDB; A5DRX1; -.
DR   SMR; A5DRX1; -.
DR   STRING; 379508.A5DRX1; -.
DR   EnsemblFungi; EDK41929; EDK41929; LELG_00107.
DR   GeneID; 5235945; -.
DR   KEGG; lel:LELG_00107; -.
DR   VEuPathDB; FungiDB:LELG_00107; -.
DR   eggNOG; KOG4020; Eukaryota.
DR   HOGENOM; CLU_067152_0_1_1; -.
DR   InParanoid; A5DRX1; -.
DR   OrthoDB; 1588798at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR031838; Dre2_N.
DR   Pfam; PF16803; DRE2_N; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome.
FT   CHAIN           1..313
FT                   /note="Fe-S cluster assembly protein DRE2"
FT                   /id="PRO_0000392392"
FT   REGION          1..184
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   REGION          134..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..270
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   REGION          187..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000250|UniProtKB:P36152"
FT   COMPBIAS        187..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34790 MW;  0F51D82C1F7D6298 CRC64;
     MTLRILLLLH PTVVSDQNLV ESVKSKISAE HPNHSLDQQI INRITQGDVV LSNNTYDEIH
     YINPNDSQYL EMPILLIKLL NDLLTHDGVL RGDLPKDQNL DALMQGFVVG DDGSWIKPKP
     VETVLLLKKK KESNITSNSN NNDSSPREVG VNNTGNYTHA AMSTLASKKK IPMFKKLLDR
     SNEVKGNLAS GTVKSPSPGL TDTSAQNTDE ENENGNSMKR KLVETKLTYF SDSDSDNNEG
     RDLDDDDDDG QEDNDIYINE NDLISELKSD NLIIPKKCEL PQWGKGAERH VRTVRVGLKG
     VVKEAGAFRR QSG