ID   A0A397HYR8_9EURO        Unreviewed;       712 AA.
AC   A0A397HYR8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Ferric oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01794};
GN   ORFNames=CDV56_108921 {ECO:0000313|EMBL:RHZ67158.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ67158.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ67158.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ67158.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHZ67158.1}.
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DR   EMBL; NKHU02000008; RHZ67158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397HYR8; -.
DR   STRING; 41047.A0A397HYR8; -.
DR   VEuPathDB; FungiDB:CDV56_108921; -.
DR   OrthoDB; 2444729at2759; -.
DR   Proteomes; UP000215305; 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   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:UP000215305};
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        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          286..402
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   712 AA;  80763 MW;  0DEF0DDFD536C977 CRC64;
     MKLLKYQRAA QVLVSLGIPV ASHDPNGRPG YGLIGYGISM YRPLCAYACR ASITNPLDCN
     KTADHNMDMS SMEMDTPSPS CYANNDPFLQ TLAYCMYTHC ADLSVSVLEN YWELNVAGRL
     QHQPSPKESY QEALGSLAKP PTTTLNTSEV LDIASLVVEE TYLSNCDTLS TFEAVETSHE
     RYGLVLLLTG AIIPIASSLL RFVPFPAAWR VRFSAIFIDP PFIGRRHSSP IFDTFYMPTR
     GQALFIAYLS IINIILCAVG FRSAQPNTWY ASKHDEILTY VANRVGVLSF ANIPLLVLYT
     GRNNFLLWLT DWSHSTFLLL HRWLAFICTL EACLHSAIYL QIYVANNEHS TESRLPYWIW
     GVVATLALAI LIPSSTWPIR KRFYELFLAW HVILSFFALL ACYWHIWYRY GHQWGYETWI
     YIAFGIWAFE RGFRLLRLAR HGMRKAYVTV LDDEYLKVEV PGVHAQGHVY LYFPTLTWRV
     WENHPFSAIA SLRRENSLEK IAIEAQDVKG EHLSKNGLSV TTFLDQGKMP SSSSTPSSRD
     LTGDRYYQPC LTLFVRTQSG ITRHLRARSQ LPVLVEGSYP LSPLTSDHWS DHPNVIAIAG
     GVGITALLPD LCSHRGRHAL FWASRSKALI DSVQETVGNT CLHNRDMKIY HDRRMDIPKL
     LREEMQKYRG VPVCVVVSGP AGMADEVRLV VSEMVRENPS LLVSFVEESF SW
//