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Database: UniProt
Entry: U7Q7P1_SPOS1
LinkDB: U7Q7P1_SPOS1
Original site: U7Q7P1_SPOS1 
ID   U7Q7P1_SPOS1            Unreviewed;       651 AA.
AC   U7Q7P1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=HMPREF1624_01058 {ECO:0000313|EMBL:ERT02756.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT02756.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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; KI440842; ERT02756.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7Q7P1; -.
DR   STRING; 1391915.U7Q7P1; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_019268_1_0_1; -.
DR   OrthoDB; 2043195at2759; -.
DR   Proteomes; UP000018087; 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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; 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; 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   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:UP000018087};
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:ARBA00023065}.
FT   TRANSMEM        28..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          296..456
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          60..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  72249 MW;  25413995CB22C299 CRC64;
     MAWPWEFLEL SPEERQARRL VLDRYGHYGA LFSVSPIVVM LLVRITLWTV AFVRMRYGQS
     LRGSSRGSPG SSSSNARYDA VPDSPSLKSR RLTTRGSWES WYRRAKWWLS DDVVIFRQHL
     GQRDLWVGGG SWMAILLVLC VVETGRDYMH LTKRFGIVAV SQLPLQYVLA LRYVSPVLAI
     FGTSHEQVNR WHRVLGTIIY TMLLLHATFY LNFFAFLGNF WPRLLRPVVA LGLAAIFSMT
     LLTTTALSIV RRWSYRVFFI THVSVAFALP VLVIFHARYA SNYVAAALLL LIADLTFRKI
     QTVTTEARIE TIPGTELIRL TAPIPFSKMD KYRKHPGSHV YMSLPGSARP STNPLSPTSI
     LFEFLFNPFT IATVNDQSSD LTLVVRARKG PMSAALSRHA CPVQLTKNAD GRAEDDDDDE
     TTPAIPTIHG LGTASNMGTG TMSVNLEGPY GSSAYFPELT PHNFDRVLLV AGGVGATFVV
     PLYRSIIDET AAIRNGGSLK VDLVWSVRGA GDATWAVVSG QDGSGHSLLQ DRNVHIFLTG
     GGTGSAAVAE NSAAEAAIEL TTLRRDQQAT SPRGRRPQSS PQSRFVPPGA SNRQRPDFSQ
     IVDDVFRHGS EERVAVLVCG PEAMVQDLRA SVSMWVHRGR SVWWHNESFG W
//
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