##gff-version 3 ##sequence-region Q9H1K1 1 167 Q9H1K1 UniProtKB Transit peptide 1 34 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H1K1 UniProtKB Chain 35 167 . . . ID=PRO_0000019692;Note=Iron-sulfur cluster assembly enzyme ISCU Q9H1K1 UniProtKB Active site 69 69 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D7P6 Q9H1K1 UniProtKB Active site 138 138 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O29689 Q9H1K1 UniProtKB Binding site 71 71 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:31101807,ECO:0007744|PDB:6NZU;Dbxref=PMID:31101807 Q9H1K1 UniProtKB Binding site 95 95 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:31101807,ECO:0007744|PDB:6NZU;Dbxref=PMID:31101807 Q9H1K1 UniProtKB Binding site 138 138 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:31101807,ECO:0007744|PDB:6NZU;Dbxref=PMID:31101807 Q9H1K1 UniProtKB Site 35 35 . . . Note=Mediates ISCU dimerization and de novo [2Fe-2S] cluster assembly;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34824239;Dbxref=PMID:34824239 Q9H1K1 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine%3B by MTOR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23508953;Dbxref=PMID:23508953 Q9H1K1 UniProtKB Modified residue 69 69 . . . Note=Cysteine persulfide;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D7P6 Q9H1K1 UniProtKB Modified residue 138 138 . . . Note=Cysteine persulfide;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Alternative sequence 1 38 . . . ID=VSP_013492;Note=In isoform 2. MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKK->MVLIDMSVDLSTQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11060020;Dbxref=PMID:11060020 Q9H1K1 UniProtKB Natural variant 12 12 . . . ID=VAR_060728;Note=A->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:11060020,ECO:0000269|PubMed:15489334,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=dbSNP:rs2287555,PMID:11060020,PMID:15489334,PMID:18669648,PMID:19413330,PMID:20068231,PMID:23186163,PMID:24275569 Q9H1K1 UniProtKB Mutagenesis 14 14 . . . Note=Loss of phosphorylation. Does not affect phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23508953;Dbxref=PMID:23508953 Q9H1K1 UniProtKB Mutagenesis 35 35 . . . Note=Does not affect mitochondrial localization. Loss of iron-sulfur cluster biogenesis. Does not affect reductive cleavage of the ISCU2-bound-persulfide by FDX2. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34824239;Dbxref=PMID:34824239 Q9H1K1 UniProtKB Mutagenesis 69 69 . . . Note=Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Slightly decreases the cysteine desulfurase activity in the presence of FXN%3B when associated with A-95. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN%3B when associated with A-95. Loss of the [2Fe-2S] cluster formation. C->A Q9H1K1 UniProtKB Mutagenesis 69 69 . . . Note=Does not affect the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 71 71 . . . Note=Stabilizes the D-state. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23940031;Dbxref=PMID:23940031 Q9H1K1 UniProtKB Mutagenesis 71 71 . . . Note=Stabilizes the S-state. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23940031;Dbxref=PMID:23940031 Q9H1K1 UniProtKB Mutagenesis 95 95 . . . Note=Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Slightly decreases the cysteine desulfurase activity in the presence of FXN%3B when associated with A-95. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN%3B when associated with A.69. Loss of the [2Fe-2S] cluster formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 95 95 . . . Note=Slightly decrease the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 122 122 . . . Note=Stabilizes the S-state. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23940031;Dbxref=PMID:23940031 Q9H1K1 UniProtKB Mutagenesis 130 130 . . . Note=Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect the [2Fe-2S] cluster assembly. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 137 137 . . . Note=Stabilizes the D-state. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23940031;Dbxref=PMID:23940031 Q9H1K1 UniProtKB Mutagenesis 138 138 . . . Note=Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Loss of iron-based stimulation of the cysteine desulfurase activity in the presence of FXN. Loss of the [2Fe-2S] cluster formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 138 138 . . . Note=Loss of iron-based stimulation of the cysteine desulfurase activity in the presence of FXN. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24971490;Dbxref=PMID:24971490 Q9H1K1 UniProtKB Mutagenesis 140 140 . . . Note=Does not affect the SDA complex formation. Abolishes desulfurase activity of SDA complex when zinc ion is bound. Activated by FXN when component of SDAU complex. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30031876;Dbxref=PMID:30031876 Q9H1K1 UniProtKB Mutagenesis 140 140 . . . Note=Does not affect the SDA complex formation. Abolishes desulfurase activity of SDA complex when zinc ion is bound. Activated by FXN when component of SDAU complex. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30031876;Dbxref=PMID:30031876 Q9H1K1 UniProtKB Mutagenesis 140 140 . . . Note=Does not affect the SDA complex formation. Abolishes desulfurase activity of SDA complex when zinc ion is bound. Activated by FXN when component of SDAU complex. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30031876;Dbxref=PMID:30031876 Q9H1K1 UniProtKB Sequence conflict 7 7 . . . Note=F->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H1K1 UniProtKB Helix 37 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WLW Q9H1K1 UniProtKB Beta strand 59 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Beta strand 83 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 96 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 114 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 122 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Helix 136 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UXE Q9H1K1 UniProtKB Binding site 46 46 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29097656,ECO:0007744|PDB:5WLW;Dbxref=PMID:29097656 Q9H1K1 UniProtKB Binding site 70 70 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29097656,ECO:0007744|PDB:5WLW;Dbxref=PMID:29097656 Q9H1K1 UniProtKB Binding site 112 112 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29097656,ECO:0007744|PDB:5WLW;Dbxref=PMID:29097656