ID   AIM14_YEAS1             Reviewed;         570 AA.
AC   B3LHL3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
DE   AltName: Full=Altered inheritance of mitochondria protein 14;
GN   Name=AIM14; ORFNames=SCRG_01152;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408044; EDV10371.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LHL3; -.
DR   EnsemblFungi; EDV10371; EDV10371; SCRG_01152.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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..570
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408751"
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          481..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  65822 MW;  7D5FE43FC98A2971 CRC64;
     MKESPLITLV KRHSETHFAN IKYGYYVLII SLVYLIGLAL LRAFGRRTPS RSSSAFKNKI
     IYRLYDIDPA IHLGILFFAV LIPFYYHYSL 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 KTYTLINSYP
     PSVPEECYSQ GTNIAIICGG SGISFALPLF RHFFNKENVK YLKMIWLIKN YSEYELVLDY
     LKTNGLTFEK KLSNNKRISV FISGEYTAET RLDEITTNID DENSEYEMGS FNNEDEDLSI
     SNFNSENADS NDNTPETSHS PTKENGSLIE VKSKHSFTLS SELKSFNNES AQVNQNETWL
     FSCGPPSLLQ LSKKYCNDER INFVCETYGL