ID A0A1E5RGN5_9ASCO Unreviewed; 759 AA.
AC A0A1E5RGN5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative ferric reductase transmembrane component 8 {ECO:0000313|EMBL:OEJ86068.1};
GN ORFNames=AWRI3579_g1099 {ECO:0000313|EMBL:OEJ86068.1};
OS Hanseniaspora osmophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ86068.1, ECO:0000313|Proteomes:UP000095728};
RN [1] {ECO:0000313|Proteomes:UP000095728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEJ86068.1}.
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DR EMBL; LPNM01000006; OEJ86068.1; -; Genomic_DNA.
DR InParanoid; A0A1E5RGN5; -.
DR OrthoDB; 2056230at2759; -.
DR Proteomes; UP000095728; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR PANTHER; PTHR11972:SF208; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 8-RELATED; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SFLD; SFLDF00463; AIM14; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095728};
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 TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..273
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT REGION 528..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 86905 MW; 4CA534C1FBA94196 CRC64;
MSAQNIQTLM APPESPEAGS YKRVFFDLIR LPDFQHKLEW EFSHSLIAKS ANXTFXLALF
IICGLIPLAN YLSLKFPKIN MFFSHYHKHN RNLYQRRRSS NTNLDPAANT FFHKWHKFIN
KKISSVIYNT SLKQFLLWGT IVSVCSTWRN YGDLINITKR LGRISCALYP PLLCLTLRPS
PLPHTMYLNL IPVHKWISRI VILTSFLHTV FYFSYFIYFN SLFKVLKWAN FTGVLAMCCF
IIIGVTSLRL VRRGNFTFFY SNHYICTWIS VVLLDIHSRP TIKWFTAMNY ILLVGQIFYR
LYHTKKCDKV SIVNISSNLS IMEFDKKYMT KQPEYPSSHV RINNLYHESN HVLQNWCKLI
WYTVIPLQHP FTVASLPNED NVRLIIRKXN FPLIDQAPYA ITGSFESKVP FLHKPNKAPH
YIASSLTSPV SPLLFDESHG KKKFYIDARK VLIVVGGSAI SFGLPLLRVL NYNGINCKLI
WVTRDYQDLC LLNYFQKNFY GLEIYITGED FKNEQDLGID YVDYEDEDDE ENLTNSVNNQ
QSSNPANTGY GSISRLKKHL DSKPNIPNTP QNQPVSATIT TDSADDEIDF TNFHTNKQVK
DKKSDKKLGS HNSTLPEQKS NFRKPSVVFP PSVDTSYGQE TRIQVPSGVC VNFGRPTLGA
KEYVWCLEGD CDVSMIQAAL FEEGFCVEGT LEQEDLRADE HSTLNEGNAT GSSSAGKGGI
TPEKLSKTWV VAAGPQGLVD SAKKWSLEHG FQFHDEVYF
//
