ID IND1_YARLI Reviewed; 312 AA. AC Q6CE48; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Iron-sulfur protein IND1; DE AltName: Full=Iron-sulfur protein required for NADH dehydrogenase 1; DE Flags: Precursor; GN Name=IND1; OrderedLocusNames=YALI0B18590g; 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). RN [2] RP PROTEIN SEQUENCE OF 35-38, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF CYS-242; CYS-245 AND CYS-279. RX PubMed=18497740; DOI=10.1038/emboj.2008.98; RA Bych K., Kerscher S., Netz D.J.A., Pierik A.J., Zwicker K., Huynen M.A., RA Lill R., Brandt U., Balk J.; RT "The iron-sulphur protein Ind1 is required for effective complex I RT assembly."; RL EMBO J. 27:1736-1746(2008). CC -!- FUNCTION: Required for the effective assembly of the mitochondrial CC membrane respiratory chain NADH dehydrogenase (Complex I). Probably CC facilitates the assembly of Fe-S cofactors and subunits of complex I. CC {ECO:0000269|PubMed:18497740}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:18497740}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:18497740}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:18497740}; Peripheral membrane protein CC {ECO:0000269|PubMed:18497740}; Matrix side CC {ECO:0000269|PubMed:18497740}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {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; CR382128; CAG83317.1; -; Genomic_DNA. DR RefSeq; XP_501064.1; XM_501064.1. DR AlphaFoldDB; Q6CE48; -. DR SMR; Q6CE48; -. DR STRING; 284591.Q6CE48; -. DR EnsemblFungi; CAG83317; CAG83317; YALI0_B18590g. DR GeneID; 2907193; -. DR KEGG; yli:YALI0B18590g; -. DR VEuPathDB; FungiDB:YALI0_B18590g; -. DR HOGENOM; CLU_024839_0_2_1; -. DR InParanoid; Q6CE48; -. DR OMA; VSGCPMR; -. DR OrthoDB; 228512at2759; -. DR Proteomes; UP000001300; Chromosome B. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central. DR CDD; cd02037; Mrp_NBP35; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR000808; Mrp-like_CS. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR044304; NUBPL-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033756; YlxH/NBP35. DR PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1. DR PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01215; MRP; 1. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Nucleotide-binding; Reference proteome; Transit peptide. FT TRANSIT 1..34 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:18497740" FT CHAIN 35..312 FT /note="Iron-sulfur protein IND1" FT /id="PRO_0000352527" FT REGION 32..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 75..82 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MUTAGEN 242 FT /note="C->A,E,S: Reduces the amount of fully assembled FT complex I." FT /evidence="ECO:0000269|PubMed:18497740" FT MUTAGEN 245 FT /note="C->A,E,S: Reduces the amount of fully assembled FT complex I." FT /evidence="ECO:0000269|PubMed:18497740" FT MUTAGEN 279 FT /note="C->A,S: No effect." FT /evidence="ECO:0000269|PubMed:18497740" FT MUTAGEN 279 FT /note="C->E: Abolishes most of complex I activity." FT /evidence="ECO:0000269|PubMed:18497740" SQ SEQUENCE 312 AA; 33167 MW; 25F5F96432C8A327 CRC64; MRGFRLIAPI QRSIAIISRL QPITANFHSS PALRSHENPL GIPKSPASAP RIPRKTTRRP EPIAGVKKTI VVSSAKGGVG KSTVSVNTAL SLAKRGLRVG LLDVDIFGPS IPTMFGLSGE PRMTHEGKLI PMSKFGIQVM SMGFLVDPNK AVAWRGLLVQ KALEQLLQDV DWGTLDVLVM DLPPGTGDVQ LTIAQTVKID GAIIVSTPQD VALVDVVRGL DLFEKTYTKV LGLVQNMSVF VCPNCNHETH IFGVDGAVSK AKSRGLGVLG NVPLDPQICS QSDKGVPVAV SGGVQAKYYD KIAEGVAEQL GV //