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Database: UniProt
Entry: M7TXF3_BOTF1
LinkDB: M7TXF3_BOTF1
Original site: M7TXF3_BOTF1 
ID   M7TXF3_BOTF1            Unreviewed;       715 AA.
AC   M7TXF3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000256|ARBA:ARBA00039906};
DE   AltName: Full=Iron-sulfur clusters transporter atm1, mitochondrial {ECO:0000256|ARBA:ARBA00040792};
GN   ORFNames=BcDW1_5380 {ECO:0000313|EMBL:EMR85929.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85929.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Heavy Metal importer (TC 3.A.1.210) subfamily.
CC       {ECO:0000256|ARBA:ARBA00024363}.
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DR   EMBL; KB707876; EMR85929.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TXF3; -.
DR   SMR; M7TXF3; -.
DR   STRING; 1290391.M7TXF3; -.
DR   HOGENOM; CLU_000604_84_1_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   CDD; cd18582; ABC_6TM_ATM1_ABCB7; 1.
DR   CDD; cd03253; ABCC_ATM1_transporter; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF402; IRON-SULFUR CLUSTERS TRANSPORTER ABCB7, MITOCHONDRIAL; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        127..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..417
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          452..688
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          50..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  78743 MW;  161A269422FC6D05 CRC64;
     MSFRSLHSFH GASCIYAKAS LRHPQWAKPG VGLRVFTSTN RLLKDIPKGS AIQSQSLRNP
     KTADDIPGAT PETAKKAPLA IPTTARKDPL ALDDKTNKEQ RKADWAIIKE MSQYLWPKDN
     MGTRVRVGLS LGLLVGAKVL NVQVPFYFKS IVDAMNVDFA TLGGTATTVA GSMILAYGLT
     RIGATLFQEV RNAVFASVAQ KAIRRVACNV FDHLLRLDLN FHLSKQTGGL TRAIDRGTKG
     ISFLLTSMVF HIFPTVLEIS MVCGILTYQY GAKFAAITAL TMVGYTAFTI STTAWRTKFR
     RAANAADNKG STVAVDSLIN YEAVKYFNNE KYEVGRYDQA LKAYEKSSIK VATSLAFLNS
     GQNLIFSSAL TAMMYLAADG VATGNLTVGD LVMVNQLVFQ LSVPLNFLGS VYRELRQSLL
     DMETLFNLQK VNVAVREAPN AKPLQLTKGG EITFENVTFG YHPDRPILKN LSMTIPAGKK
     IAIVGPSGCG KSTVLRLLFR FYDVQEGRIL IDGQDIRNVS LESLRRAIGV VPQDTPLFND
     SIEHNIRYGN LEASDEKVKE AAQRAKIHSI ITTLPDGYKT MVGERGMMIS GGEKQRLAVS
     RLILKDPPLL FFDEATSALD THTEQALMQN INSILKEKSR TSVFVAHRLR TIFDSDKIIV
     LKDGSVAENG THRELVDTGG VYSDLWSVQE TLFAETEKGK EQEVNTPDVS KEESR
//
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