DRE2_AJEDR
ID DRE2_AJEDR Reviewed; 359 AA.
AC C5GYL7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=BDCG_09508;
OS Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER-3 / ATCC MYA-2586;
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999988; EEQ86239.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GYL7; -.
DR STRING; 559297.C5GYL7; -.
DR EnsemblFungi; EEQ86239; EEQ86239; BDCG_09508.
DR VEuPathDB; FungiDB:BDCG_09508; -.
DR eggNOG; KOG4020; Eukaryota.
DR HOGENOM; CLU_067152_1_0_1; -.
DR OMA; KRPINIP; -.
DR Proteomes; UP000002039; Unassembled WGS sequence.
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;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Fe-S cluster assembly protein DRE2"
FT /id="PRO_0000392375"
FT REGION 1..148
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..246
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 149..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..272
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 322..336
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 322..325
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 333..336
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT COMPBIAS 168..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 267
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 272
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 322
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 325
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 333
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ SEQUENCE 359 AA; 38541 MW; EEBB23A9FF2C1401 CRC64;
MASTGRVLLL SPPSLSSHPE KLNAILGSHT RDRTDLQMLD RLVHGLVSLP ASTYDIVLLL
TGADNTLAEP YSLVTRDIIQ QVVHSLKPAG KLRSQDNKAW GLRSSGNNSD DDNDNDELTF
RNEAILAGLV FDDNGELLKP DVAAQQAVPL KLGRRKKEKE RRHPSGNDVT NGKVNAPSSN
GVNASTSTAT ATATTTTTTT PKTNPAPSGV GFIDFSDDYG VPMEEDPQGS DDELIDEDEL
LGEDDMGRPI VQPPECRPKP GKRRRACKDC SCGLSQKLEA EDKAKRATAD KALETIMAPT
MKLGSSELAE VDFTVQGKVG SCGNCSLGDA FRCDGCPYIG LPAFKPGEEV RLLNNDVQL
