ATM1_ASPFU
ID ATM1_ASPFU Reviewed; 727 AA.
AC Q4WLN7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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}; ORFNames=AFUA_6G12870;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL89127.1; -; Genomic_DNA.
DR RefSeq; XP_751165.1; XM_746072.1.
DR AlphaFoldDB; Q4WLN7; -.
DR SMR; Q4WLN7; -.
DR STRING; 746128.CADAFUBP00000182; -.
DR PRIDE; Q4WLN7; -.
DR EnsemblFungi; EAL89127; EAL89127; AFUA_6G12870.
DR GeneID; 3508472; -.
DR KEGG; afm:AFUA_6G12870; -.
DR VEuPathDB; FungiDB:Afu6g12870; -.
DR eggNOG; KOG0057; Eukaryota.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; Q4WLN7; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 248727at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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: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:0006811; P:ion transport; IEA:UniProtKB-KW.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..727
FT /note="Iron-sulfur clusters transporter atm1,
FT mitochondrial"
FT /id="PRO_0000255438"
FT TOPO_DOM ?..130
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 153..175
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 200..248
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 273
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 295..360
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 380..394
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 395..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 417..727
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 131..421
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 456..692
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 46..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 300..304
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 363..366
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 413
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 489..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 727 AA; 80659 MW; 2BE3A6E561542880 CRC64;
MLPGAARSPC LRFPRRFAHG GLAAPRTALW ATAWYGIHSK AFTSANSPLR KDASKEPALA
SNSKTTNPIP TQASASVNPP KDARNATTAK KDLLSETTLA NKEQRKADWA IIKEMAKYLW
PKDDWGTKLR VGTALSLLVG AKILNVEVPF YFKSIVDSMN IDFATVGGTA YTVAGSMIIA
YGVTRIGATL FQELRNAVFA SVAQKAIRRV ARNVFEHLLR LDLNFHLSRQ TGGLTRAIDR
GTKGISFLLT SMVFHVVPTA LEISLVCGIL TYQYGFQFAA ITAATMVAYT AFTITTTAWR
TKFRKQANAA DNRGATVAVD SLINYEAVKY FNNEQYQVAR YDKALKAYED ASIKVTTSLA
FLNSGQNMIF SSALAAMMYL AANGVANGNL TVGDLVMVNQ LVFQLSVPLN FLGSVYRELR
QSLLDMETLF NLQKVNVNIK EKPDAKPLQL HKGGEIRFEN VTFGYHPDRP ILKNASFTIP
AGQKFAIVGP SGCGKSTILR LLFRFYDVQE GRILIDDQDV RDVSLESLRK AIGVVPQDTP
LFNDTIAHNI RYGRIDATDE EVHKAAQRAR IDALIQKLPE GYQTAVGERG MMISGGEKQR
LAISRLILKD PELLFFDEAT SALDTYTEQA LLQNINSILK EKKRTSVFVA HRLRTIYDSD
QILVLKDGRV AEMGSHRELL DLNGIYAELW NAQEMSLAQD LEFERETERD DVESKERDMA
PGPKAQQ
