ISA1_SCHPO
ID ISA1_SCHPO Reviewed; 190 AA.
AC P78859;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Iron-sulfur assembly protein 1;
GN Name=isa1; ORFNames=SPCC645.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=11941510; DOI=10.1007/s00775-001-0330-2;
RA Wu G., Mansy S.S., Hemann C., Hille R., Surerus K.K., Cowan J.A.;
RT "Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces
RT pombe Isa1.";
RL J. Biol. Inorg. Chem. 7:526-532(2002).
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:11941510}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; D89209; BAA13870.1; -; mRNA.
DR EMBL; CU329672; CAB39899.1; -; Genomic_DNA.
DR PIR; T43013; T43013.
DR RefSeq; NP_588112.1; NM_001023102.2.
DR AlphaFoldDB; P78859; -.
DR SMR; P78859; -.
DR BioGRID; 275974; 3.
DR STRING; 4896.SPCC645.03c.1; -.
DR MaxQB; P78859; -.
DR PaxDb; P78859; -.
DR EnsemblFungi; SPCC645.03c.1; SPCC645.03c.1:pep; SPCC645.03c.
DR GeneID; 2539409; -.
DR KEGG; spo:SPCC645.03c; -.
DR PomBase; SPCC645.03c; isa1.
DR VEuPathDB; FungiDB:SPCC645.03c; -.
DR eggNOG; KOG1120; Eukaryota.
DR HOGENOM; CLU_069054_0_2_1; -.
DR InParanoid; P78859; -.
DR OMA; CAGQAYS; -.
DR PhylomeDB; P78859; -.
DR Reactome; R-SPO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:P78859; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:PomBase.
DR GO; GO:0036455; F:iron-sulfur transferase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; ISS:PomBase.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:PomBase.
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 2: Evidence at transcript level;
KW Iron; Metal-binding; Mitochondrion; Reference proteome.
FT CHAIN 1..190
FT /note="Iron-sulfur assembly protein 1"
FT /id="PRO_0000077036"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ SEQUENCE 190 AA; 21222 MW; 4A3E1C562DFAED2E CRC64;
MLSCLSKPAL RCRSVNRLQF LRKLSLQEIQ TLKTQHQYLG RTRLDVETPS LKPSAAGSGS
TAPKPVTERE IASTRFMPRK NVIKLTPLAV EHLKKMQSSA SMKGKMLRIG VKQKGCAGQA
YSLEYIEKPD KFDEIVKQDG ISIIVARRAL LQIIGSVMDY RDDDLQSRFI FSNPNVKSTC
GCGESFSTLK
