ISA1_YEAST
ID ISA1_YEAST Reviewed; 250 AA.
AC Q07821; D6VXX7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Iron-sulfur assembly protein 1;
GN Name=ISA1; OrderedLocusNames=YLL027W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=10748136; DOI=10.1074/jbc.m909502199;
RA Kaut A., Lange H., Diekert K., Kispal G., Lill R.;
RT "Isa1p is a component of the mitochondrial machinery for maturation of
RT cellular iron-sulfur proteins and requires conserved cysteine residues for
RT function.";
RL J. Biol. Chem. 275:15955-15961(2000).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Involved in the assembly of mitochondrial and cytoplasmic
CC iron-sulfur proteins. Probably involved in the binding of an
CC intermediate of Fe/S cluster assembly. {ECO:0000269|PubMed:10748136}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; Z73132; CAA97476.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09293.1; -; Genomic_DNA.
DR PIR; S64778; S64778.
DR RefSeq; NP_013073.1; NM_001181847.1.
DR AlphaFoldDB; Q07821; -.
DR SMR; Q07821; -.
DR BioGRID; 31225; 81.
DR DIP; DIP-1394N; -.
DR IntAct; Q07821; 5.
DR MINT; Q07821; -.
DR STRING; 4932.YLL027W; -.
DR MaxQB; Q07821; -.
DR PaxDb; Q07821; -.
DR PRIDE; Q07821; -.
DR EnsemblFungi; YLL027W_mRNA; YLL027W; YLL027W.
DR GeneID; 850632; -.
DR KEGG; sce:YLL027W; -.
DR SGD; S000003950; ISA1.
DR VEuPathDB; FungiDB:YLL027W; -.
DR eggNOG; KOG1120; Eukaryota.
DR GeneTree; ENSGT00490000043385; -.
DR HOGENOM; CLU_069054_0_1_1; -.
DR InParanoid; Q07821; -.
DR OMA; FWRGGTN; -.
DR BioCyc; YEAST:G3O-32131-MON; -.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q07821; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07821; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISA:SGD.
DR GO; GO:0009102; P:biotin biosynthetic process; IMP:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IMP:SGD.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR Gene3D; 2.60.300.12; -; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
DR PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Mitochondrion; Reference proteome.
FT CHAIN 1..250
FT /note="Iron-sulfur assembly protein 1"
FT /id="PRO_0000077034"
FT REGION 54..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ SEQUENCE 250 AA; 27675 MW; 226C286B4F80DE6D CRC64;
MINTGRSRNS VLLAHRFLST GGFWRGGTNG TMSRTINNVN PFKLKFIPKT VPAAADSVSP
DSQRPGKKPF KFIVSNQSKS SKASKSPKWS SYAFPSRETI KSHEEAIKKQ NKAIDEQIAA
AVSKNDCSCT EPPKKRKRKL RPRKALITLS PKAIKHLRAL LAQPEPKLIR VSARNRGCSG
LTYDLQYITE PGKFDEVVEQ DGVKIVIDSK ALFSIIGSEM DWIDDKLASK FVFKNPNSKG
TCGCGESFMV
