ID A0A2N6NJ51_BEABA Unreviewed; 761 AA.
AC A0A2N6NJ51;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE SubName: Full=Ferric reductase transmembrane component 3 {ECO:0000313|EMBL:PMB67317.1};
GN Name=FRE3_0 {ECO:0000313|EMBL:PMB67317.1};
GN ORFNames=BM221_006981 {ECO:0000313|EMBL:PMB67317.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB67317.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB67317.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB67317.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(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:PMB67317.1}.
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DR EMBL; MRVG01000007; PMB67317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NJ51; -.
DR OMA; CIDTYCP; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013130; Fe3_Rdtase_TM_dom.
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 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.
PE 4: Predicted;
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:UP000235728};
KW 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:ARBA00023065}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..761
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014950824"
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..448
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT REGION 142..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83990 MW; 29C32690647AD432 CRC64;
MAAFNLGHWL LIAAIPAVLG DGIGIIGFGT TMYQPFCAYA CRSVIDRSPL LCTPEHEGYS
AGGHHAPAIT PESCFARDPA FAQTLALCID TYCPGSDAPR LGEIEEYWAS HLATGMMGNF
SWVPAMTYQE ALLRARHDEH NSTLAGNTTT STSGHAGHGK RVNLARHGSH AEEEEDTTPV
NTTLPVLKPG APLNVTSFVR PSDWLKNYNG HKSFELNEIG HSKYTIIITV VPFLLAILAS
LPRFIPGLTR ATSWAWFNSM IIYPPLWGKR HRQPTAQVIG GGFMPTRGQS LYILVMVALN
IVFLMVPYYT LQPQTTFVTV REQELSVIGC RAGVMAMGNV VVLTVFAGRN NPLLALTGWN
YDTYLLLHRT FGYLAIFHTV VHSVLLLAYY VMFGDYQAEL VRLYWIWGIV ATMAVVLLWP
ASMLVVRRRF YEVFLSVHHL LVALFLIGYF YHVFYRYSFK WGYEIWCYIA GGIWGTERLI
RLVRMVFMGR RTADVFVVPG CEGEYLRIDI DGAHATGLVY LYFPTLSWRF WENHPFSVAS
SFSISDSSED DSTDAESPND GLAEEKKLPT NIETAPVAPP RRTIVTPVSS HRISILVRVQ
AGMTARLAAR VTAGGSKIRL PVVVEGSYHA ISASELSQCT SIVCIAGGVG VSAVLSILRE
KGCRRRLCWG VRDSSVVDEC KKDILNLPAA VQVDISVGQR LDIRSILKEE LLARTGDCGP
VGVVVCGPPG MADDVRNEVS RLARSGSLAR GVVLLDEAFT W
//
