ID   AIM14_ASHGO             Reviewed;         516 AA.
AC   Q754F4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; OrderedLocusNames=AFR116W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53487.1; -; Genomic_DNA.
DR   RefSeq; NP_985663.1; NM_211017.1.
DR   AlphaFoldDB; Q754F4; -.
DR   STRING; 33169.AAS53487; -.
DR   PRIDE; Q754F4; -.
DR   EnsemblFungi; AAS53487; AAS53487; AGOS_AFR116W.
DR   GeneID; 4621910; -.
DR   KEGG; ago:AGOS_AFR116W; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; Q754F4; -.
DR   OMA; LIPLHKW; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
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:0006915; P:apoptotic process; IEA:EnsemblFungi.
DR   GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:EnsemblFungi.
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   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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   SUPFAM; SSF63380; SSF63380; 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..516
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408740"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          94..207
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          238..363
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
SQ   SEQUENCE   516 AA;  58495 MW;  607B208203A4BA8E CRC64;
     MDGQVTVKRH GDTHFANIGY GYYTFGVSVG YILLLLLLRK RRGTAVPRSR HKLFQMMIDG
     SPALHLPILL LFLEIAFLGH YSVIDHASVY IKRLGRLSYV LLFLNIFLTL RPNYILSDYT
     YVQLLPMHMW LSRAISTFGV FHGLAFVIKW QLDNEVSLAS KLFNLWNLLG FIVWILLIIL
     LITSTGVIRR RSYKSFYMVH QINAFAISFI VPVHARPGVA LPYTITIAVL LGLHALARVS
     FCMSSAVVHK LSNYQKGSKL VRIKLPRNVM PEHFTPGSHI RVSPYRRSNP LYWLVPSHPF
     TIASLPDDDH VDLILREHGH FEFEVGPRYS IVHNYEGITA LQLGLVNRVT IVVGGTGISL
     GLPLFRYFKE NTDIGYLKMI WTVKSHADLH VLDDFEGIDI FVTQNTTTTP IPGASESWDE
     IPLEEFELNS MDDLEAEEEH LGESGALLPT TKRKKDPGAI NIGRRLDWNV ELASFVRSEG
     SSDQLLIVCG PESLVKDGVQ FATDHNIVFY KEVYSF