ATM1_YARLI
ID ATM1_YARLI Reviewed; 710 AA.
AC Q6C6N0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000305};
DE EC=7.-.-.- {ECO:0000250|UniProtKB:Q2G506};
DE Flags: Precursor;
GN Name=ATM1 {ECO:0000305}; OrderedLocusNames=YALI0E08030g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Performs an essential function in the generation of
CC cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export
CC of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial
CC proteins (By similarity). Hydrolyzes ATP (By similarity). Binds
CC glutathione and may function by transporting a glutathione-conjugated
CC iron-sulfur compound (By similarity). {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; CR382131; CAG79271.1; -; Genomic_DNA.
DR RefSeq; XP_503682.1; XM_503682.1.
DR AlphaFoldDB; Q6C6N0; -.
DR SMR; Q6C6N0; -.
DR STRING; 4952.CAG79271; -.
DR EnsemblFungi; CAG79271; CAG79271; YALI0_E08030g.
DR GeneID; 2912473; -.
DR KEGG; yli:YALI0E08030g; -.
DR VEuPathDB; FungiDB:YALI0_E08030g; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q6C6N0; -.
DR OMA; VTEWRTH; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..710
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /id="PRO_0000255450"
FT TOPO_DOM 39..129
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 152..173
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 174..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 198..246
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 247..270
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 271
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 293..358
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 378..392
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 393..414
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 415..710
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 130..419
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 453..687
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 35..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298..302
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 361..364
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 411
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 486..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 710 AA; 77390 MW; E88626826C7A940B CRC64;
MWLSLPRSGY GSVATLTSKR VLACLTPLRQ FSTSPAVSNA NHKNVDNINK SPANDAANNA
VEKGDKPTTS PEKLATKAEK SSANSVKAAA NALGESNLSN SEQRRLDWII MKDMLKYIWP
KGKTSVKFRV LVAVALLVGA KLLNVQVPFF FKEIIDDMNI EWNSATALGV GITALIFSYG
AARFGAVLFG ELRNAIFASV AQKAIKEVAT NVFRHLLKLD MAFHLSRQTG GITRAIDRGT
KGISFVLSSM VFHIIPIALE ISLVCGILSY NFGWKYALVT GATMVSYAIF TITTTSWRTK
FRRNANRADN EASNVCLDSL INIEAVKSFG NEGYMVDKYQ SALTKYEKAS IKIATSLAFL
NSGQNLIFSS ALTAMMYMTC CGVADGSLTV GDLVLVNQLV FQLSVPLNFL GSVYRDLRQS
LLDMGSLFSL QKVAGQIQES PNAKPLQLTN GEIRFENVTY GYHPDRPILK NASFVIPGGL
KTAIVGPSGS GKSTILKLAF RFYDTQEGRI LIDGQDVREV TLASLRSAIG VVPQDTPLFN
DSIMNNIRFG RLEADDKEVE NAACAAKLDA LVRQLPDGWN TNVGERGMMI SGGEKQRLAV
ARVLLKNSPV VFLDEATSAL DTNTERQLLA NMDQVLGDKT CVAIAHRLRT VADSDKIICL
NQGGVEEEGT QAELLLKDGL YKSMWDAQEQ VELGEEGIKE AEEKAAKKDV
