ID   AIM14_DEBHA             Reviewed;         512 AA.
AC   Q6BM09;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; OrderedLocusNames=DEHA2F09240g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89103.2; -; Genomic_DNA.
DR   RefSeq; XP_460762.2; XM_460762.1.
DR   AlphaFoldDB; Q6BM09; -.
DR   SMR; Q6BM09; -.
DR   STRING; 4959.XP_460762.2; -.
DR   EnsemblFungi; CAG89103; CAG89103; DEHA2F09240g.
DR   GeneID; 2903598; -.
DR   KEGG; dha:DEHA2F09240g; -.
DR   VEuPathDB; FungiDB:DEHA2F09240g; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; Q6BM09; -.
DR   OMA; LIPLHKW; -.
DR   OrthoDB; 936110at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR   GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
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.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   PROSITE; PS51384; FAD_FR; 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..512
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408744"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          94..206
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          230..355
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          427..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  58691 MW;  64CBFC3B437EA91A CRC64;
     MNELESFSPR HEGHHHAANI KYGYIVLGFS VVHIIGILIC KSVFKLRWTT STKGIDFVKS
     PLFISIIAWT LILIGLGVFH VQLPENYVTS IKRFGRMSYA LLPFDIFLVL RPNSIGLRYL
     ELMDLHKWMS RVIIAGAIIH GVGYFIKWIL EGSLFTKSVR LWNFLGIVVF MLNLILIIIS
     LRYFRRRIYQ YFYVVHNITV WLFVGLICLH ARPGVGKYAI ACASLLGLQI FERYAKSHSI
     SDLKVISYEG SNLIVVRIQR DSKIADWPSG SHIRLTYPLT NYRSWIFPTH PYTIASLESD
     EMLDLIISKS NRFILHPQMP YSWTGPFTSF SKELLQTIDN VDIICGGSGI SFALPVFRNL
     KQKASHVKLI WCVRSNNDLH VLRTLNFNEE IIIHITGNLQ DSTSNTIFDE EDYGLLDYDN
     NENFELESLP SSETPSRTVN DDSLSQDTRP KKESKFIIVQ GRPDFGNTFE SLVQVNSSNK
     WIIACGPRSL VNSAQEWASE NKVNFVSEIY EM