ID   AIM14_CANDC             Reviewed;         537 AA.
AC   B9WB34;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; ORFNames=CD36_18260;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992689; CAX43604.1; -; Genomic_DNA.
DR   RefSeq; XP_002418304.1; XM_002418259.1.
DR   AlphaFoldDB; B9WB34; -.
DR   SMR; B9WB34; -.
DR   STRING; 42374.XP_002418304.1; -.
DR   EnsemblFungi; CAX43604; CAX43604; CD36_18260.
DR   GeneID; 8045859; -.
DR   KEGG; cdu:CD36_18260; -.
DR   CGD; CAL0000170048; Cd36_18260.
DR   VEuPathDB; FungiDB:CD36_18260; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   OrthoDB; 936110at2759; -.
DR   Proteomes; UP000002605; Chromosome 2.
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.
DR   SUPFAM; SSF52343; SSF52343; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW   Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..537
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408741"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          97..213
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          187..363
FT                   /note="FAD-binding FR-type"
FT   REGION          432..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  61960 MW;  16F1EBDC3B480140 CRC64;
     MEEVVVPRHG DHHNINIKYG FFIFALTIIQ TIFFLQVKFI QIKRWNSTGR FSKFWSQITN
     PPIWLMVTVW LLIVIFTGGH KISDFSEEYI ISAKRYGRMA YCLIPLNIYL VLRPTNSPLL
     KPGYYLENMS LHKWTSRIIV FCSTIHAAGY VYKWIKEGAI LNKPFRFLNL LGVVVFVFLV
     VLAIISIRPF RRKVYSTFYL IHNVTAWSMV ILITFHARPG VTVFAVISLI LLGYQLYLRY
     YSSYMVNSLK VIDIPTSTLQ IIKIPQSNKF PNWLPGSHIR LNYTISKFKS WTTASHPFTV
     VTIPEDSTNN LTLIVRKPNS FVINPLDSYL VTGPYPSLAP PFFTTANIVN IICGGSGISL
     GLPIYHHFKS INSTVPVKLV WTIRNQNDTF IMNQLDMTGV QVYVTSIGDT NSEQQENQQQ
     AVPLFVIEEE EEEQGHGLLN NDNENGIELQ NMPKTNEESS EANSTNSKNN KDNQERKEYF
     KFGRPKFDEV FAIDDPTTTY DLDNSWVIAC GPDELISDAK RWSKDRGYRF YYEKYEM