ID Q6CET4_YARLI Unreviewed; 688 AA.
AC Q6CET4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=YALI0B13134p {ECO:0000313|EMBL:CAG83079.1};
GN ORFNames=YALI0_B13134g {ECO:0000313|EMBL:CAG83079.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG83079.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG83079.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; CR382128; CAG83079.1; -; Genomic_DNA.
DR RefSeq; XP_500828.1; XM_500828.1.
DR AlphaFoldDB; Q6CET4; -.
DR EnsemblFungi; CAG83079; CAG83079; YALI0_B13134g.
DR GeneID; 2907537; -.
DR KEGG; yli:YALI0B13134g; -.
DR VEuPathDB; FungiDB:YALI0_B13134g; -.
DR HOGENOM; CLU_010365_4_0_1; -.
DR InParanoid; Q6CET4; -.
DR OMA; YDGWTRH; -.
DR OrthoDB; 2477110at2759; -.
DR Proteomes; UP000001300; Chromosome B.
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:0015677; P:copper ion import; IBA:GO_Central.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 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 PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..688
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012542531"
FT TRANSMEM 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..529
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 688 AA; 78271 MW; 24F8241A3F093DB7 CRC64;
MRLTSLLALA TVALAGRRDK PGDKMLVDTS AVAGALSKSA KFGVDPGETN LEYYNNYWAC
PQYMATLMIW YRAVVPDEEQ WKKVLQSDIV ETYNEYGKMH LTLDEVVAVY ENGTKYVETP
KNASAIVYAP VPFNQTGYDE YYPTVKEFYK QLDLGTYYGG GLLAYWLAIF LIGMFTNLAK
HAFFGIYQKM KGHRFRKHVS LPALWGYKHC QTSGGWLGGF ISMCTPTRAQ SLAVAGYLIM
AFIFCFTQFD LFTPNYYFEA NGDQLARYLA DRTGIMAMTQ IPIVFLFGGR NNFFMWLTGW
SFDTFNIYHR YSSRVMVVYA IIHSICYSYI ERGSYFAIAS SQFYWIMGVV ATICGSLILF
QGLHFFRSRW YETFLVIHLV LAVAFLVGMW YHCRTLGWMQ YLYATIAVWS FDRFARIVRI
FWSGFVVSGD FELVDPDQLI VKAEMDYSKW WSIYPGVHVY IYILNGKFWE SHPFTVYQSP
FAEETGKMTV LLKAKEGKTL SLANLLAKGD GKRRLKTLIE GPYGSKHPIG KYDSSIYVAG
GIGITATYSY AVDVIKKSTA KTLVFTWVVR NETCLTWFKT ELDTLLADPR VEVNLYVTGN
HTDIPPLGGS ESDSKNSEKS VSEMNPRLNI VYGRPDMTVE MPAYIERCAG STAIVVCGPP
VLNDDIRLSL VQSADCSKVD YYEEAFSW
//
