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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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