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AIM14_VANPO
ID   AIM14_VANPO             Reviewed;         519 AA.
AC   A7TQE6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; ORFNames=Kpol_467p2;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480457; EDO15490.1; -; Genomic_DNA.
DR   RefSeq; XP_001643348.1; XM_001643298.1.
DR   AlphaFoldDB; A7TQE6; -.
DR   SMR; A7TQE6; -.
DR   STRING; 436907.A7TQE6; -.
DR   EnsemblFungi; EDO15490; EDO15490; Kpol_467p2.
DR   GeneID; 5543595; -.
DR   KEGG; vpo:Kpol_467p2; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; A7TQE6; -.
DR   OMA; LIPLHKW; -.
DR   OrthoDB; 936110at2759; -.
DR   PhylomeDB; A7TQE6; -.
DR   Proteomes; UP000000267; 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.
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..519
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408749"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          88..207
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          237..366
FT                   /note="FAD-binding FR-type"
SQ   SEQUENCE   519 AA;  59833 MW;  0321926B6C01734A CRC64;
     MDELVKRHGS THFANINYGY YILFLSIIYI ILLFCLRNYA KITTRSTRFF KKLYSLNPFI
     HLSILLIAIF IPFYQPHLNK LTVYYKRLGR LSYTLIPLNL FLTLKPNWFL PSQCTYTDFI
     PIHKWLSRFI TFIAILHSIL FLSHWSSSSD ENVSIAIKLQ NPKNVLGLIM LIPSLLLICL
     SIGPFRRFSY TSFYIIHNIS NVMLIFLTPI HARPGVAIPY LIINSILLLA IAFNKIFFIK
     KSELLAKETL PNYDNNSSLV TIRLPRSALP ETFTPACHIR ISPYQFFNPL YWLLPSHPYT
     VVSLPSDDSV DLVLTENIKK FAFRLHMERS YTIINQFNPS VPIACLNSSK RVCIVCGGTG
     ISFGLPLYRY FSEIIERNQR SIEYLRLIWM VKDKSQIKIL EKLNSLKYDL EDKNFTSNFH
     VFITQYSSKS SGIEDSSGSG YELEDLTPED PSSIGPYIFG SVNFGRRIEW TTDLSTFVEH
     DNDIDNTWML ACGPSTLVES ANKYADKSGV RFASEIYTL
 
 
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