DRE2_LEIMA
ID DRE2_LEIMA Reviewed; 113 AA.
AC Q4QIS1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Anamorsin homolog;
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
GN ORFNames=LmjF07.0230, LmjF_07_0230;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
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 cytosolic Fe-S
CC scaffold complex. Electrons are transferred from NADPH via a FAD- and
CC FMN-containing diflavin oxidoreductase. Together with the diflavin
CC oxidoreductase, also required for the assembly of the diferric tyrosyl
CC radical cofactor of ribonucleotide reductase (RNR), probably by
CC providing electrons for reduction during radical cofactor maturation in
CC the catalytic small subunit. {ECO:0000250|UniProtKB:P36152}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P36152};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P36152};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6FI81}.
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 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:0000250|UniProtKB:P36152}.
CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR796403; CAJ06982.1; -; Genomic_DNA.
DR RefSeq; XP_001680927.1; XM_001680875.1.
DR AlphaFoldDB; Q4QIS1; -.
DR STRING; 5664.LmjF.07.0230; -.
DR EnsemblProtists; CAJ06982; CAJ06982; LMJF_07_0230.
DR GeneID; 5649179; -.
DR KEGG; lma:LMJF_07_0230; -.
DR VEuPathDB; TriTrypDB:LmjF.07.0230; -.
DR VEuPathDB; TriTrypDB:LMJLV39_070008200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_070008400; -.
DR eggNOG; KOG4020; Eukaryota.
DR InParanoid; Q4QIS1; -.
DR OMA; TMPPGGC; -.
DR Proteomes; UP000000542; Chromosome 7.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR PANTHER; PTHR13273; PTHR13273; 1.
DR Pfam; PF05093; CIAPIN1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..113
FT /note="Anamorsin homolog"
FT /id="PRO_0000392365"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..113
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT REGION 42..54
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT REGION 75..89
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT MOTIF 75..78
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT MOTIF 86..89
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 54
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36152"
SQ SEQUENCE 113 AA; 12194 MW; 39EEA3B42A767E66 CRC64;
MSSPAPSTQA FSLKTRQPIP DEDALLTEED RILKQATKGE DCTTRRRACK NCVCGRAELE
RKLEAEVLTM PPGGCGNCSK GDAFRCAGCP FLGQPAFDAT EDGKVKLNLT DDV
