DRE2_PYRTR
ID DRE2_PYRTR Reviewed; 316 AA.
AC B2W1T4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=PTRG_04419;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU47257.1; -; Genomic_DNA.
DR RefSeq; XP_001934752.1; XM_001934717.1.
DR AlphaFoldDB; B2W1T4; -.
DR SMR; B2W1T4; -.
DR STRING; 45151.EDU47257; -.
DR PRIDE; B2W1T4; -.
DR EnsemblFungi; EDU47257; EDU47257; PTRG_04419.
DR GeneID; 6342659; -.
DR eggNOG; KOG4020; Eukaryota.
DR HOGENOM; CLU_067152_1_0_1; -.
DR InParanoid; B2W1T4; -.
DR OMA; KRPINIP; -.
DR OrthoDB; 1588798at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
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..316
FT /note="Fe-S cluster assembly protein dre2"
FT /id="PRO_0000392403"
FT REGION 1..128
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 129..208
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 141..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..234
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 279..293
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 279..282
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 290..293
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 218
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 229
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 232
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 234
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 279
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 293
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ SEQUENCE 316 AA; 33807 MW; 7C3487C665A701AB CRC64;
MAPRCLLIGT PSIAAHPERL DQVYEIHHRS STDLQMLDRI AAGLVNLPAA TYDVVLLLAD
ADGTTRESHK LFSRDVMNKV ASALKIGGVL KSQAGPFQGA EKTEAILAGL TETEDGMAKP
EQEEPVSIPL KFGKNKANGV SATNGTNGAV NPDGSVPLNL NRKRDQPEPV KPAGVGFVDF
SDDLDDPIIT GEDDDLIDED DLITEADMAR PVVQPLECQP KPGKRRRACK DCTCGMKEKL
EAEDAAKRSS ADKALNSLKL DADDLAEVDF TVQGKVGSCG NCALGDAFRC DGCPYIGLPA
FKPGEEVRLL NNDIQL
