##gff-version 3
Q9UMS0	UniProtKB	Transit peptide	1	9	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9UMS0	UniProtKB	Chain	10	254	.	.	.	ID=PRO_0000166191;Note=NFU1 iron-sulfur cluster scaffold homolog%2C mitochondrial	
Q9UMS0	UniProtKB	Region	173	241	.	.	.	Note=NifU	
Q9UMS0	UniProtKB	Binding site	210	210	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27818104;Dbxref=PMID:27818104	
Q9UMS0	UniProtKB	Binding site	213	213	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27818104;Dbxref=PMID:27818104	
Q9UMS0	UniProtKB	Alternative sequence	1	141	.	.	.	ID=VSP_041224;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9UMS0	UniProtKB	Alternative sequence	1	24	.	.	.	ID=VSP_041225;Note=In isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10810093,ECO:0000303|PubMed:11342215,ECO:0000303|PubMed:12886008;Dbxref=PMID:10810093,PMID:11342215,PMID:12886008	
Q9UMS0	UniProtKB	Natural variant	21	21	.	.	.	ID=VAR_079757;Note=In MMDS1%3B patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25918518;Dbxref=dbSNP:rs776875884,PMID:25918518	
Q9UMS0	UniProtKB	Natural variant	25	25	.	.	.	ID=VAR_044429;Note=M->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12915448,ECO:0000269|PubMed:14702039;Dbxref=dbSNP:rs4453725,PMID:12915448,PMID:14702039	
Q9UMS0	UniProtKB	Natural variant	182	182	.	.	.	ID=VAR_079758;Note=In MMDS1%3B patient's skin fibroblasts show deficiency of lipoic acid synthase and reduced lipoic acid content. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25918518;Dbxref=dbSNP:rs1354126704,PMID:25918518	
Q9UMS0	UniProtKB	Natural variant	189	189	.	.	.	ID=VAR_079759;Note=In MMDS1%3B alters protein structure%3B increases likelihood of existing as monomer%3B decreases ability to receive a Fe/S clusters from donor proteins%3B decreases delivery rates of [2Fe-2S] cluster to target proteins. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25918518,ECO:0000269|PubMed:28906594;Dbxref=PMID:25918518,PMID:28906594	
Q9UMS0	UniProtKB	Natural variant	190	190	.	.	.	ID=VAR_079760;Note=In MMDS1%3B uncertain significance. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25918518;Dbxref=PMID:25918518	
Q9UMS0	UniProtKB	Natural variant	208	208	.	.	.	ID=VAR_066639;Note=In MMDS1%3B patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes%3B increases homodimerization%3B unable to receive a Fe/S clusters from donor proteins%3B changes delivery rates of [2Fe-2S] cluster to target proteins. G->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22077971,ECO:0000269|PubMed:25918518,ECO:0000269|PubMed:28161430;Dbxref=dbSNP:rs374514431,PMID:22077971,PMID:25918518,PMID:28161430	
Q9UMS0	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Alters protein structure. Increases likelihood of existing as monomer. Decreases ability to receive a Fe/S clusters from donor proteins. Decreases delivery rates of [2Fe-2S] cluster to target proteins. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28906594;Dbxref=PMID:28906594	
Q9UMS0	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Alters protein structure. Increases likelihood of existing as monomer. Decreases ability to receive a Fe/S clusters from donor proteins. Decreases delivery rates of [2Fe-2S] cluster to target proteins. G->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28906594;Dbxref=PMID:28906594	
Q9UMS0	UniProtKB	Sequence conflict	158	158	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9UMS0	UniProtKB	Beta strand	62	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Beta strand	71	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Beta strand	80	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Beta strand	86	88	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Helix	93	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Helix	98	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Beta strand	109	115	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Beta strand	118	125	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Helix	130	147	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LTM	
Q9UMS0	UniProtKB	Helix	167	188	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O	
Q9UMS0	UniProtKB	Beta strand	192	198	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O	
Q9UMS0	UniProtKB	Beta strand	201	206	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O	
Q9UMS0	UniProtKB	Turn	208	212	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O	
Q9UMS0	UniProtKB	Helix	214	231	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O	
Q9UMS0	UniProtKB	Beta strand	237	240	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M5O