NFU1_DROPE
ID NFU1_DROPE Reviewed; 282 AA.
AC B4H303;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=NFU1 iron-sulfur cluster scaffold homolog, mitochondrial {ECO:0000250|UniProtKB:Q9UMS0};
DE Flags: Precursor;
GN ORFNames=GL13432;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW30835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC mitochondrial iron-sulfur proteins. {ECO:0000250|UniProtKB:Q9UMS0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; CH479205; EDW30835.1; -; Genomic_DNA.
DR RefSeq; XP_002025336.1; XM_002025300.1.
DR AlphaFoldDB; B4H303; -.
DR SMR; B4H303; -.
DR STRING; 7234.FBpp0177539; -.
DR EnsemblMetazoa; FBtr0179047; FBpp0177539; FBgn0151038.
DR eggNOG; KOG2358; Eukaryota.
DR HOGENOM; CLU_060555_0_2_1; -.
DR OMA; AIMEHYM; -.
DR PhylomeDB; B4H303; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 3.30.1370.70; -; 1.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01106; NifU; 1.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF110836; SSF110836; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 3: Inferred from homology;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..282
FT /note="NFU1 iron-sulfur cluster scaffold homolog,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388699"
FT REGION 178..246
FT /note="NifU"
FT /evidence="ECO:0000255"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS0"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS0"
SQ SEQUENCE 282 AA; 31129 MW; DFD2BC3E41E887E4 CRC64;
MSKLLSYTAR IILRNSRITV RQLVRGFAGF VSGQRNAPQP AYGRPVPGLL RQKMVSSIGK
RSMFIQTQDT PNPDSLKFLP GVEVLGKGNT YDFPSGTAAH CSPLAKLLFR VEGVRAVFFG
SDFITISKEE SAEWSLIKPE VFAVIMDFFA SGLPILHEAR PNADTEILDD DDETVMMIKE
LLDTRIRPTV QEDGGDIVFI SYENGVVKLK MQGSCSSCPS SIVTLKNGVQ NMLQFYIPEV
ESVEQVFDDA DRMADKEFER FEKNLKQKEP AGAPVGIGGG PN
