ID   AIM14_YEAS8             Reviewed;         576 AA.
AC   C8Z891;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
DE   AltName: Full=Altered inheritance of mitochondria protein 14;
GN   Name=AIM14; ORFNames=EC1118_1G1_1200g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC       iron or copper homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ribosomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC       subfamily. {ECO:0000305}.
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DR   EMBL; FN393070; CAY79607.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z891; -.
DR   EnsemblFungi; CAY79607; CAY79607; EC1118_1G1_1200g.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome VII, Scaffold EC1118_1G1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW   Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..576
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408754"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          101..219
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          250..388
FT                   /note="FAD-binding FR-type"
FT   REGION          480..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  66645 MW;  7533BBF54D10018D CRC64;
     MKESPLITLV KRHSETHFAN IKYGYYVLII SLVYLIGLAL LRAFGRRTPS RSSSAFKNKI
     IYRLYDIDPA IHLGILFFAV LVPFYYHYSL TTQSTVYLKR LGRLSYALIP LNLFLTLRPN
     WFLRKNCTYT DFIPFHKWFS RIITVIGLLH GIFFIIKWAI DDNVSLKQKL ILKTFNFVGF
     IISILVLFLL ICSIGPMRRY NYRLFYIVHN LVNVAFILLT PIHSRPGVKF PFLLLNCTLL
     FIHIINRIVF AKSLMILNKN ANYSKTNLVH VRLPRAILPD YFEPGSHIRI SPYRRINPLY
     WLLPSHPYTI ASLAEDNSID LIIKETSTAE PGSQIESLRS NPKSFHLDQE KNYTLINSYP
     PSVPEECYSQ GTNIAIICGG SGISFALPLF RHFFNKENVK YLKMIWLIKN YSEYELVLDY
     LKTNGLTFEK KLSNNKRISV FISGEYTAET RLDEITTNID DENSEYEMGS FNNEDEDLSI
     SNFNSENADS NDNTPETSHS PTKENGSLIE VKSKHSFTLS NELKSFNNES AQVNQNETWL
     FSCGPPSLLQ LSKKYCNDER INFSVRLTDY EGKRKE