DRE2_CANGA
ID DRE2_CANGA Reviewed; 338 AA.
AC Q6FTJ8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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};
GN OrderedLocusNames=CAGL0G01947g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380953; CAG59373.1; -; Genomic_DNA.
DR RefSeq; XP_446446.1; XM_446446.1.
DR AlphaFoldDB; Q6FTJ8; -.
DR SMR; Q6FTJ8; -.
DR STRING; 5478.XP_446446.1; -.
DR EnsemblFungi; CAG59373; CAG59373; CAGL0G01947g.
DR GeneID; 2888420; -.
DR KEGG; cgr:CAGL0G01947g; -.
DR CGD; CAL0130709; CAGL0G01947g.
DR VEuPathDB; FungiDB:CAGL0G01947g; -.
DR eggNOG; KOG4020; Eukaryota.
DR HOGENOM; CLU_067152_0_0_1; -.
DR InParanoid; Q6FTJ8; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0097361; C:CIA complex; IEA:EnsemblFungi.
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:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IEA:EnsemblFungi.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:1905118; P:positive regulation of ribonucleoside-diphosphate reductase activity; IEA:EnsemblFungi.
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;
KW Reference proteome.
FT CHAIN 1..338
FT /note="Fe-S cluster assembly protein DRE2"
FT /id="PRO_0000324860"
FT REGION 1..165
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 166..232
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 181..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..258
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 301..315
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 301..304
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 312..315
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 242
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 253
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 256
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 258
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 301
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 304
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ SEQUENCE 338 AA; 37064 MW; 667A1F732CD70BF3 CRC64;
MAKSGLLLIH PAITTTPEEV EKAKADAVAA DVKIANQFLI NKVNEGSVKL QKGIYDVIYY
LTPEAPDAIL FPKKLIGALN EALKVGGVLY GLSDKYKIDA LVNDFDIVSD SGKYHWVKKV
NMAVKAEPVA VPLKKSEKSE PSKTLPSFKK AGESKLPSFK KAANKPLPTF KKKVEEAKPK
VEARVHKAEN DDDELEDEED ENLFDASRSK YFDEDDSESL DEDDLLNEED AKNIGGITMI
TCGKSKTKKK KACKDCSCGI KEEEEAEIDN IRSQQDTVVK FTEDELTEID FTIDGKKVGG
CGSCSLGDAF RCTGCPYLGL PAFKPGEPIN LDSITDDL
