ID   AIM14_YARLI             Reviewed;         525 AA.
AC   Q6C188;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; OrderedLocusNames=YALI0F18348g;
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: Probable cell surface metalloreductase. May be involved in
CC       iron or copper homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR382132; CAG78383.1; -; Genomic_DNA.
DR   RefSeq; XP_505574.1; XM_505574.1.
DR   AlphaFoldDB; Q6C188; -.
DR   SMR; Q6C188; -.
DR   STRING; 284591.Q6C188; -.
DR   EnsemblFungi; CAG78383; CAG78383; YALI0_F18348g.
DR   GeneID; 2907808; -.
DR   KEGG; yli:YALI0F18348g; -.
DR   VEuPathDB; FungiDB:YALI0_F18348g; -.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; Q6C188; -.
DR   OMA; LIPLHKW; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR   GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..525
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408750"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          82..194
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          215..344
FT                   /note="FAD-binding FR-type"
FT   REGION          407..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..437
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58630 MW;  0FEFFD5DA2CF98E6 CRC64;
     MLEKRHGDHH NANIKYGTFV LVISLLVVCY IAVRNLTQPE VRARTKRDLR LPLWLSVLLW
     TALVIGMGVI HVEELNEAAK RFGRLCYALL PLIVFLAIRP SPLPRTFYLK LLPLHKWLGR
     LATLVGVVHG VLYTVHFVKK NEFYKVFKFD NFLGVIILAV FLVMVVTSLP FFRKRMYSLF
     YTIHYLSAWF VAIATIFHAR PGVGWLFFWV ALFMGSSLLY RVLASSTVQI ESTEAMGPDL
     HRVTFPRSIL PEFFVPASHI RVSRTLRNPL SWISSTHPYT ISSLPSDDHV ELIVRPTKFS
     LAHAASGTQF AVYGPFESLP DDFFSTANRV LVFAGGAGIS FALPVVQTLA KAGISHKLVW
     VLRNKAGVSE VESRLGETPT DIYITGQDPF LGEGVVYAKD AEGTAGLLSE DMEMEEIGQE
     DEDRERDELD DLLSEDEGSS SQDSTKGAHK NKGKDQDNGK REASQSITYH DGRPQPADTA
     SAYFLDRSAP EGKWILACGP NGLVVTAEQA AKKTGVRFCN ETYSM