(data stored in ACNUC7421 zone)

SWISSPROT: ATM1_ASHGO

ID   ATM1_ASHGO              Reviewed;         691 AA.
AC   Q751N2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 114.
DE   RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial;
DE   Flags: Precursor;
GN   Name=ATM1; OrderedLocusNames=AGL335W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. Hydrolyzes ATP. Binds glutathione and may function by
CC       transporting a glutathione-conjugated iron-sulfur compound (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {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}.
DR   EMBL; AE016820; AAS54156.1; -; Genomic_DNA.
DR   RefSeq; NP_986332.1; NM_211394.1.
DR   SMR; Q751N2; -.
DR   STRING; 33169.AAS54156; -.
DR   PRIDE; Q751N2; -.
DR   EnsemblFungi; AAS54156; AAS54156; AGOS_AGL335W.
DR   GeneID; 4622625; -.
DR   KEGG; ago:AGOS_AGL335W; -.
DR   InParanoid; Q751N2; -.
DR   KO; K05663; -.
DR   OMA; VTEWRTH; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
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:0048250; P:iron import into the mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_I_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;
DR   PRODOM; Q751N2.
DR   SWISS-2DPAGE; Q751N2.
KW   ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..691
FT                   /note="Iron-sulfur clusters transporter ATM1,
FT                   mitochondrial"
FT                   /id="PRO_0000255437"
FT   TOPO_DOM        23..109
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        132..154
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        155..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        179..227
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        228..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        252
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        274..339
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        340..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        359..373
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        374..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        396..691
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          110..400
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          435..671
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   NP_BIND         468..479
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          279..283
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000250"
FT   REGION          342..345
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /note="Glutathione; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   691 AA;  76821 MW;  908631BA33F69B64 CRC64;
     MFRLLRFSPS RYYPRSMAPV RWSTHPYHVT APRMWGTRMP LQLQASLRPN NAVEKGISGD
     VKVAGAMVKP AASGGESAKS KTPTVSELKI LKDLFRYIWP RGDRKVKTRV LIALGLLLGS
     KLLNVQVPFF FKSTVDSMNI EWGDVGTALP IAVTLTVLSY GAARFGAVLF VELRNAVFSN
     VAQSAITKVS LQTFQHLMKL DLGWHLSRQT GGLTRAMDRG CKGISYVLSA MVFHIIPITF
     EISMVCGILT YQFGASFAAI TFSTMLLYSI FTFRTTAWRT RFRRDANKAD NKAASVALDS
     LINFEAVKYF NNEKYLADKY HTSLMKYRDS QIKVSQSLAF LNTGQNLIFT TALTAMMYMA
     CNGVMQGSLT VGDLVLINQL VFQLSVPLNF LGSVYRDLKQ SLIDMESLFK LQKNQVTIKN
     SPNAQNLPIH KPLDIRFENV TFGYDPERRI LNNVSFTIPA GMKTAIVGPS GSGKSTILKL
     VFRFYEPEQG RILVGGTDIR DLDLLSLRKA IGVVPQDTPL FNDTIWENVK FGNISSSDDE
     ILRAIEKAQL TKLLQNLPKG ASTVVGERGL MISGGEKQRL AIARVLLKDA PLMFFDEATS
     ALDTHTEQAL LHTIQQNFSS NSKTSVYVAH RLRTIADADK IIVLEQGSVR EEGTHSSLLA
     SQGSLYRGLW DIQENLTLPE RPEQSTGSQH A
//

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