ID B9WMD0_CANDC Unreviewed; 709 AA.
AC B9WMD0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Ferric reductase transmembrane component, putative {ECO:0000313|EMBL:CAX40243.1};
DE EC=1.16.1.7 {ECO:0000313|EMBL:CAX40243.1};
GN OrderedLocusNames=Cd36_32920 {ECO:0000313|CGD:CAL0000169249};
GN ORFNames=CD36_32920 {ECO:0000313|EMBL:CAX40243.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40243.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40243.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992695; CAX40243.1; -; Genomic_DNA.
DR RefSeq; XP_002422239.1; XM_002422194.1.
DR AlphaFoldDB; B9WMD0; -.
DR GeneID; 8049388; -.
DR KEGG; cdu:CD36_32920; -.
DR CGD; CAL0000169249; Cd36_32920.
DR VEuPathDB; FungiDB:CD36_32920; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_4_0_1; -.
DR OrthoDB; 2477110at2759; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
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 ECO:0000313|EMBL:CAX40243.1}; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..709
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002893969"
FT TRANSMEM 155..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 420..531
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 612..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 81511 MW; E276546C7ED36004 CRC64;
MRIFYCLVLL SFSLINVSGM SMSYERYHDY LGFYTCNRQI KKSITFCGKS SNYTCLCSNS
NSLATYAGCL SHNHRNSTKQ KQKLVSFCAH YGGVEVDSNW YDNAIANYMA NGKYASEIEN
FNKSVPLKVP FKFTNKELDL YAAAYVQYLS NYDNAVYYGA SLLGYWLLIM CASSIFYWSK
FLFPQLTKRL TCTPINIWRK YISVPATFTK KKCQQQSCFK FFDFLIPTRF ESIAIAGFYV
LVIIVHSINM EFIKGDPFLL NKYSAQMRYV ADRTGIVATV MMPLIFLFAG RNNFLQWITG
WNYNTFMTYH RHIARVMFML IVIHAVCYTI TLKPTYTSEM KEPYLIWGVI ATVCGGIILF
QALLYFRRNW YEAFLLIHIV MAALFVAGTW IHVVDFGYVW FVYPTVAVWC FDRLIRIIRL
IYFGFPVAEV KLLTDDHSED VALRVTIPKP KYWKSIPGGH VFIHFLKPAY FWQSHPFTFV
DSTVNDGYIV CYCKIKAGIT RALYQALKNA PDRCMSIRVG VEGPYGEPTP ARYADTCVFI
AGGNGIPGIY SEIVDIANKQ KSSKEEGCTQ RLKLIWVIRK YNMLSWFHNE LANLKNTNLE
VVIYVTQSTQ RDSADHDNDK FTKSSDSLSK SANDTDSSLS TLSHVKFPDG RPCLVDIIKQ
EITESNGSVA FVSCGHPAMV DEIRYQISQN INNVENKRVD FYEQLQIWA
//
