ID E4V222_ARTGP Unreviewed; 639 AA.
AC E4V222;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=FreB protein {ECO:0000313|EMBL:EFR04087.1};
GN ORFNames=MGYG_07094 {ECO:0000313|EMBL:EFR04087.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989827; EFR04087.1; -; Genomic_DNA.
DR RefSeq; XP_003171095.1; XM_003171047.1.
DR AlphaFoldDB; E4V222; -.
DR STRING; 535722.E4V222; -.
DR GeneID; 10026342; -.
DR VEuPathDB; FungiDB:MGYG_07094; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_3_1_1; -.
DR InParanoid; E4V222; -.
DR OMA; WMDEVLR; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000002669; 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; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF12; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14340)-RELATED; 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 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:UP000002669};
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 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..484
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 383..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 70890 MW; 493DFC7635F297FB CRC64;
MELVLFAREL AAPHSQNTTY VSPYTRGLLG VRVNLDHLVT ILVAGSIGVA CVVILIVRFT
QMSHAYLRQV TSATGNNNQQ RFWGAEQSTL WSDIKKHVLY APLGSKRHNR EFKLSEAVNV
GTLPSRFHTV LLVCYLLSQV AYCSVLDYSA NNKAALVAEL RGRSGNLALL NMIPLFILAG
RNNPLIPLMR VSFDTYNLIH RWLGRIVIIE SIVHTIAWMV NAVAAEGYAK MWHGVWHEPF
YTWGFVATAA MVFILIQSPS PVRHAFYETF LHLHQIGAMV IVLGIYFHLD IDGLPQLPWF
KGIISLWAIE RGARFFRILR LNVSRRNGLT RVVVKALPGE ASRVTFYLPR HTKINPGSHV
YAYLPRISFW MSHPFSVAWA EQGSSSLPKS PKTDKFSDSS KSSLARKAST MTTSSKSSSP
DLEKGHARNT ALATDDSLPT CVSLIMAART GMTRKLYNAA LASPNLTLET TGFIEGPYSS
HPSSFGSYGT VVLFSGGAGI THHLMHVRDL LAAADAGTVA TRRVYLIWSV RTTEHLAWVR
GFMDSILHMP NRRDILVTKL FVSKPRSQRE IQSPSTTLQM FPGRCRPDVV LEEVLSDPVG
ATGVSVCGPG AFADEVRSSV RKRIGAGQVI DFVEEAFTW
//
