ID   ISU1_YARLI              Reviewed;         181 AA.
AC   Q6CFQ0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Iron sulfur cluster assembly protein 1, mitochondrial;
DE   AltName: Full=Iron sulfur cluster scaffold protein 1;
DE   Flags: Precursor;
GN   Name=ISU1; OrderedLocusNames=YALI0B04928g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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: Scaffold protein for the de novo synthesis of iron-sulfur
CC       (Fe-S) clusters within mitochondria, which is required for maturation
CC       of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins.
CC       First, a [2Fe-2S] cluster is transiently assembled on the scaffold
CC       protein ISU1. In a second step, the cluster is released from ISU1,
CC       transferred to a glutaredoxin, followed by the formation of
CC       mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and
CC       their target-specific insertion into the recipient apoproteins. Cluster
CC       assembly on ISU1 depends on the function of the cysteine desulfurase
CC       complex NFS1-ISD11, which serves as the sulfur donor for cluster
CC       synthesis, the iron-binding protein frataxin as the putative iron
CC       donor, and the electron transfer chain comprised of ferredoxin
CC       reductase and ferredoxin, which receive their electrons from NADH.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:Q9UTC6};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q9UTC6};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBUNIT: Component of the core Fe-S cluster (ISC) assembly machinery.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR   EMBL; CR382128; CAG82740.1; -; Genomic_DNA.
DR   RefSeq; XP_500512.1; XM_500512.1.
DR   AlphaFoldDB; Q6CFQ0; -.
DR   SMR; Q6CFQ0; -.
DR   STRING; 4952.CAG82740; -.
DR   PRIDE; Q6CFQ0; -.
DR   EnsemblFungi; CAG82740; CAG82740; YALI0_B04928g.
DR   GeneID; 2907434; -.
DR   KEGG; yli:YALI0B04928g; -.
DR   VEuPathDB; FungiDB:YALI0_B04928g; -.
DR   HOGENOM; CLU_079283_1_1_1; -.
DR   InParanoid; Q6CFQ0; -.
DR   OMA; YKNPRNY; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0140132; F:iron-sulfur cluster carrier activity; IEA:EnsemblFungi.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:EnsemblFungi.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   CDD; cd06664; IscU_like; 1.
DR   InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR   InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR   PANTHER; PTHR10093; PTHR10093; 1.
DR   Pfam; PF01592; NifU_N; 1.
DR   TIGRFAMs; TIGR01999; iscU; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..181
FT                   /note="Iron sulfur cluster assembly protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000019699"
FT   REGION          159..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   181 AA;  19237 MW;  DE09649167BCE5FB CRC64;
     MMFNRITRSA GLLARARPTT TAVMSPMTPL AISRRGYHEK VLDHYNNPRN VGSMNKNDED
     VGTGLVGAPA CGDVMKLQIR VDDNGVIQDV KFKTFGCGSA IASSSYVTEL VRGKSLAEAG
     KIKNTVIAKE LSLPPVKLHC SMLAEDAIKS AISDYNSKRK TKNPTLGAEA AETPAAATAT
     A