##gff-version 3
Q9NZ45	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q9NZ45	UniProtKB	Chain	2	108	.	.	.	ID=PRO_0000089803;Note=CDGSH iron-sulfur domain-containing protein 1	
Q9NZ45	UniProtKB	Transmembrane	14	31	.	.	.	Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NZ45	UniProtKB	Topological domain	32	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NZ45	UniProtKB	Active site	55	55	.	.	.	Note=Schiff-base intermediate with pyridoxal 5'-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36194135;Dbxref=PMID:36194135	
Q9NZ45	UniProtKB	Binding site	72	72	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17766439,ECO:0000269|PubMed:17766440,ECO:0000269|PubMed:17905743,ECO:0007744|PDB:2QD0,ECO:0007744|PDB:2QH7,ECO:0007744|PDB:2R13;Dbxref=PMID:17766439,PMID:17766440,PMID:17905743	
Q9NZ45	UniProtKB	Binding site	74	74	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17766439,ECO:0000269|PubMed:17766440,ECO:0000269|PubMed:17905743,ECO:0007744|PDB:2QD0,ECO:0007744|PDB:2QH7,ECO:0007744|PDB:2R13;Dbxref=PMID:17766439,PMID:17766440,PMID:17905743	
Q9NZ45	UniProtKB	Binding site	83	83	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17766439,ECO:0000269|PubMed:17766440,ECO:0000269|PubMed:17905743,ECO:0007744|PDB:2QD0,ECO:0007744|PDB:2QH7,ECO:0007744|PDB:2R13;Dbxref=PMID:17766439,PMID:17766440,PMID:17905743	
Q9NZ45	UniProtKB	Binding site	87	87	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17766439,ECO:0000269|PubMed:17766440,ECO:0000269|PubMed:17905743,ECO:0007744|PDB:2QD0,ECO:0007744|PDB:2QH7,ECO:0007744|PDB:2R13;Dbxref=PMID:17766439,PMID:17766440,PMID:17905743	
Q9NZ45	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q9NZ45	UniProtKB	Modified residue	55	55	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WS0	
Q9NZ45	UniProtKB	Modified residue	68	68	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WS0	
Q9NZ45	UniProtKB	Modified residue	104	104	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WS0	
Q9NZ45	UniProtKB	Cross-link	42	42	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	55	55	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	68	68	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	78	78	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	79	79	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	89	89	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	104	104	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	105	105	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Cross-link	106	106	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25621951;Dbxref=PMID:25621951	
Q9NZ45	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Slighly reduces the transfer rate of the [2Fe-2S] cluster. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21788481;Dbxref=PMID:21788481	
Q9NZ45	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster%3B when associated with Cys-87. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23758282;Dbxref=PMID:23758282	
Q9NZ45	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Abolishes absorption in the 300-500 nm range. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17584744;Dbxref=PMID:17584744	
Q9NZ45	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Abolishes absorption in the 300-500 nm range. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17584744;Dbxref=PMID:17584744	
Q9NZ45	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23758282;Dbxref=PMID:23758282	
Q9NZ45	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Abolishes absorption in the 300-500 nm range. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17584744;Dbxref=PMID:17584744	
Q9NZ45	UniProtKB	Mutagenesis	84	84	.	.	.	Note=Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Does not affect absorption in the 300-500 nm range. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17584744,ECO:0000269|PubMed:23758282;Dbxref=PMID:17584744,PMID:23758282	
Q9NZ45	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster%3B when associated with Ile-55. Markedly decreases the transfer rate of the [2Fe-2S] cluster. Abolishes iron transfer to the mitochondrial matrix. H->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17584744,ECO:0000269|PubMed:21788481,ECO:0000269|PubMed:23758282;Dbxref=PMID:17584744,PMID:21788481,PMID:23758282	
Q9NZ45	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Abolishes absorption in the 300-500 nm range. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17584744;Dbxref=PMID:17584744	
Q9NZ45	UniProtKB	Beta strand	47	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Beta strand	53	66	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Beta strand	68	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Beta strand	73	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Turn	78	81	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Helix	86	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF	
Q9NZ45	UniProtKB	Beta strand	98	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EZF