ISA2_YEAST
ID ISA2_YEAST Reviewed; 185 AA.
AC Q12425; D6W471;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Iron-sulfur assembly protein 2;
GN Name=ISA2; OrderedLocusNames=YPR067W; ORFNames=YP9499.22;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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=10913600; DOI=10.1016/s0014-5793(00)01711-7;
RA Pelzer W., Muhlenhoff U., Diekert K., Siegmund K., Kispal G., Lill R.;
RT "Mitochondrial Isa2p plays a crucial role in the maturation of cellular
RT iron-sulfur proteins.";
RL FEBS Lett. 476:134-139(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:10913600}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Present with 1560 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; Z71255; CAA94975.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89184.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11487.1; -; Genomic_DNA.
DR PIR; S54088; S54088.
DR RefSeq; NP_015392.1; NM_001184164.1.
DR AlphaFoldDB; Q12425; -.
DR BioGRID; 36239; 29.
DR DIP; DIP-6434N; -.
DR IntAct; Q12425; 1.
DR MINT; Q12425; -.
DR STRING; 4932.YPR067W; -.
DR MaxQB; Q12425; -.
DR PaxDb; Q12425; -.
DR PRIDE; Q12425; -.
DR EnsemblFungi; YPR067W_mRNA; YPR067W; YPR067W.
DR GeneID; 856180; -.
DR KEGG; sce:YPR067W; -.
DR SGD; S000006271; ISA2.
DR VEuPathDB; FungiDB:YPR067W; -.
DR eggNOG; KOG1119; Eukaryota.
DR GeneTree; ENSGT00390000005700; -.
DR HOGENOM; CLU_069054_1_2_1; -.
DR InParanoid; Q12425; -.
DR OMA; CHGFQYT; -.
DR BioCyc; YEAST:G3O-34215-MON; -.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q12425; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12425; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IDA: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; 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 PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Mitochondrion; Reference proteome.
FT CHAIN 1..185
FT /note="Iron-sulfur assembly protein 2"
FT /id="PRO_0000077035"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ SEQUENCE 185 AA; 20877 MW; A4719A9EC54EECF2 CRC64;
MQAKLLFTRL NFRRPSTTLR QFPLTCFLFH SKAFYSDLVT KEPLITPKRI INKTPGLNLS
ISERASNRLA EIYRNSKENL RISVESGGCH GFQYNLTLEP ATKPDIKNDV KDKEFSDDLD
DDDSKDIIYV LPEDKGRVII DSKSLNILNN TTLTYTNELI GSSFKIINGS LKSSCGCGSS
FDIEN
