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Database: UniProt
Entry: A0A1A0H6Z0_9ASCO
LinkDB: A0A1A0H6Z0_9ASCO
Original site: A0A1A0H6Z0_9ASCO 
ID   A0A1A0H6Z0_9ASCO        Unreviewed;       694 AA.
AC   A0A1A0H6Z0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=METBIDRAFT_58735 {ECO:0000313|EMBL:OBA19864.1};
OS   Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX   NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA19864.1, ECO:0000313|Proteomes:UP000092555};
RN   [1] {ECO:0000313|EMBL:OBA19864.1, ECO:0000313|Proteomes:UP000092555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA19864.1,
RC   ECO:0000313|Proteomes:UP000092555};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBA19864.1}.
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DR   EMBL; LXTC01000005; OBA19864.1; -; Genomic_DNA.
DR   RefSeq; XP_018710389.1; XM_018858303.1.
DR   AlphaFoldDB; A0A1A0H6Z0; -.
DR   STRING; 869754.A0A1A0H6Z0; -.
DR   GeneID; 30031279; -.
DR   OrthoDB; 2477110at2759; -.
DR   Proteomes; UP000092555; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
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   Reference proteome {ECO:0000313|Proteomes:UP000092555};
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        153..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          400..516
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   694 AA;  79391 MW;  7A9E2126C389761E CRC64;
     MVAMTPSRAL NGAPFIKFPS LLIAQLSCSQ VISQVNFCPS EDGSPRDFGD NSCICRNENA
     LATLAYCYQT GYPQEIESFI NMCNRDYNTS LNQGLIDAAL EKYYTAAKEL NNSSHLRYGI
     VVDFPVKLSS FTIFLYKKSY DQFLGNYNRS IDYGWYMVVY MMFVFTLAAI GNWSKLLGPK
     LVKKFTGPIL RWTRSRITLP ALSGTERTKE KHLWKVFGYL PPTRAETLAL GSFSLLALHL
     CFYKIHFVQH DPIFGTKLAA YMRYFGVRSG IIASSLLPLS VLFAGRNNIL QWFTRWEYST
     FVMFHRWISR IMVLLVIVHS VGYSKNLKFP PNHMESYIIF GVAGTVSGLA ILVQGLLVLR
     RKWYEAFLAI HIILAAAFLI GAWLHVKDFR FVWYYYVSAC LWMLDRVIRI QRLCVFGFPL
     ARVQLYEDDT LKFRVSMPPG FHAVGGGHCF VHFLRWSCFW QSHPFTYTVV NGDIVFYVKV
     KKGVTESLKR YLEENPSISA NMRVAIEGSY GEATPALRYD TSVFIAGGNG IPGIFAEAVE
     VAEYHKGHRK VKLIWAVREY KSLLWFYDEL QDLAKLDIET EIYISRPHSN LCTSVSDKLV
     LLENTYTHRS YQSTEAMEDP IQKIHHDLTN VVFKKGRPNI AKIVEISCEE SLGSTCFVTC
     GHPDMVDDIR DQVAQKVAVC PTRVDYFEQL QVWA
//
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