(data stored in ACNUC8465 zone)

SWISSPROT: ISU1_CANGA

ID   ISU1_CANGA              Reviewed;         213 AA.
AC   Q6FJY3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=CAGL0M02629g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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-
CC       sulfur (Fe-S) clusters within mitochondria, which is required for
CC       maturation of both mitochondrial and cytoplasmic [2Fe-2S] and
CC       [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently
CC       assembled on the scaffold protein ISU1. In a second step, the
CC       cluster is released from ISU1, transferred to a glutaredoxin,
CC       followed by the formation of mitochondrial [2Fe-2S] proteins, the
CC       synthesis of [4Fe-4S] clusters and their target-specific insertion
CC       into the recipient apoproteins. Cluster assembly on ISU1 depends
CC       on the function of the cysteine desulfurase complex NFS1-ISD11,
CC       which serves as the sulfur donor for cluster synthesis, the iron-
CC       binding protein frataxin as the putative iron donor, and the
CC       electron transfer chain comprised of ferredoxin reductase and
CC       ferredoxin, which receive their electrons from NADH.
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
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
CC       machinery. {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q03020}.
CC   -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
DR   EMBL; CR380959; CAG62437.1; -; Genomic_DNA.
DR   RefSeq; XP_449461.1; XM_449461.1.
DR   SMR; Q6FJY3; -.
DR   STRING; 5478.XP_449461.1; -.
DR   EnsemblFungi; CAG62437; CAG62437; CAGL0M02629g.
DR   GeneID; 2891469; -.
DR   KEGG; cgr:CAGL0M02629g; -.
DR   CGD; CAL0136631; CAGL0M02629g.
DR   EuPathDB; FungiDB:CAGL0M02629g; -.
DR   eggNOG; KOG3361; Eukaryota.
DR   eggNOG; COG0822; LUCA.
DR   HOGENOM; HOG000069228; -.
DR   InParanoid; Q6FJY3; -.
DR   KO; K22068; -.
DR   OMA; NNIGRRM; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
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;
DR   PRODOM; Q6FJY3.
DR   SWISS-2DPAGE; Q6FJY3.
KW   2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    213       Iron sulfur cluster assembly protein 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000019695.
SQ   SEQUENCE   213 AA;  22901 MW;  CC698703E5A99823 CRC64;
     MGVCVFFPLC LPCPGALTYI REAQFISSWT PADPRHKQLK MFLQRFVTVG GAAIGARSTM
     GAMGAIGAIG AKGTMNNIGR RMYHPKVIEH YTHPRNVGSM DKTLPNVGTG LVGAPACGDV
     MRLQIKVNDK TGVIEDVKFK TFGCGSAIAS SSYMTELVHG MTLDDAAKIK NTTIAKELSL
     PPVKLHCSML AEDAIKAAIK DYKSKRTSTT TLH
//

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